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Database: UniProt
Entry: Q04760
LinkDB: Q04760
Original site: Q04760 
ID   LGUL_HUMAN              Reviewed;         184 AA.
AC   Q04760; B2R6P7; B4DDV0; P78375; Q59EL0; Q5TZW3; Q96FC0; Q96J41;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 4.
DT   29-OCT-2014, entry version 156.
DE   RecName: Full=Lactoylglutathione lyase;
DE            EC=4.4.1.5;
DE   AltName: Full=Aldoketomutase;
DE   AltName: Full=Glyoxalase I;
DE            Short=Glx I;
DE   AltName: Full=Ketone-aldehyde mutase;
DE   AltName: Full=Methylglyoxalase;
DE   AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN   Name=GLO1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-111.
RX   PubMed=7684374;
RA   Kim N.-S., Umezawa Y., Ohmura S., Kato S.;
RT   "Human glyoxalase I. cDNA cloning, expression, and sequence similarity
RT   to glyoxalase I from Pseudomonas putida.";
RL   J. Biol. Chem. 268:11217-11221(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-111.
RC   TISSUE=Colon;
RX   PubMed=8449929;
RA   Ranganathan S., Walsh E.S., Godwin A.K., Tew K.D.;
RT   "Cloning and characterization of human colon glyoxalase-I.";
RL   J. Biol. Chem. 268:5661-5667(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8670058;
RA   Ridderstroem M., Mannervik B.;
RT   "Optimized heterologous expression of the human zinc enzyme glyoxalase
RT   I.";
RL   Biochem. J. 314:463-467(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-111.
RX   PubMed=10564821; DOI=10.1016/S0378-1119(99)00420-5;
RA   Ranganathan S., Ciaccio P.J., Walsh E.S., Tew K.D.;
RT   "Genomic sequence of human glyoxalase-I: analysis of promoter activity
RT   and its regulation.";
RL   Gene 240:149-155(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   VARIANTS TYR-19 AND ALA-111.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   TYR-19 AND ALA-111.
RC   TISSUE=Brain, Eye, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, CLEAVAGE OF
RP   INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT
RP   CYS-139, AND DISULFIDE BONDS.
RC   TISSUE=Erythrocyte;
RX   PubMed=20454679; DOI=10.1371/journal.pone.0010399;
RA   Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K.,
RA   Birkemeyer C.;
RT   "Posttranslational modification of human glyoxalase 1 indicates redox-
RT   dependent regulation.";
RL   PLoS ONE 5:E10399-E10399(2010).
RN   [11]
RP   IDENTIFICATION OF NITRIC OXIDE-MODIFIED FORM, PHOSPHORYLATION, AND
RP   MUTAGENESIS OF CYS-19; CYS-20; CYS-61 AND CYS-139.
RX   PubMed=17576200; DOI=10.1042/BJ20070379;
RA   de Hemptinne V., Rondas D., Vandekerckhove J., Vancompernolle K.;
RT   "Tumour necrosis factor induces phosphorylation primarily of the
RT   nitric-oxide-responsive form of glyoxalase I.";
RL   Biochem. J. 407:121-128(2007).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   FUNCTION, PHOSPHORYLATION AT THR-107, AND MUTAGENESIS OF CYS-19;
RP   CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
RX   PubMed=19199007; DOI=10.1007/s11010-009-0031-7;
RA   de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.;
RT   "Phosphorylation on Thr-106 and NO-modification of glyoxalase I
RT   suppress the TNF-induced transcriptional activity of NF-kappaB.";
RL   Mol. Cell. Biochem. 325:169-178(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP   S-BENZYL-GLUTATHIONE AND ZINC.
RX   PubMed=9218781; DOI=10.1093/emboj/16.12.3386;
RA   Cameron A.D., Olin B., Ridderstroem M., Mannervik B., Jones T.A.;
RT   "Crystal structure of human glyoxalase I -- evidence for gene
RT   duplication and 3D domain swapping.";
RL   EMBO J. 16:3386-3395(1997).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC AND
RP   S-HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVE
RP   SITE, SUBUNIT, AND MUTAGENESIS OF GLN-34; GLU-100 AND GLU-173.
RX   PubMed=9705294; DOI=10.1074/jbc.273.34.21623;
RA   Ridderstroem M., Cameron A.D., Jones T.A., Mannervik B.;
RT   "Involvement of an active-site Zn2+ ligand in the catalytic mechanism
RT   of human glyoxalase I.";
RL   J. Biol. Chem. 273:21623-21628(1998).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH
RP   S-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE;
RP   S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE AND ZINC, AND ACTIVE SITE.
RX   PubMed=10521255; DOI=10.1021/bi990696c;
RA   Cameron A.D., Ridderstroem M., Olin B., Kavarana M.J., Creighton D.J.,
RA   Mannervik B.;
RT   "Reaction mechanism of glyoxalase I explored by an X-ray
RT   crystallographic analysis of the human enzyme in complex with a
RT   transition state analogue.";
RL   Biochemistry 38:13480-13490(1999).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH SYNTHETIC
RP   INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   COFACTOR.
RX   PubMed=23122816; DOI=10.1016/j.bmcl.2012.10.045;
RA   Chiba T., Ohwada J., Sakamoto H., Kobayashi T., Fukami T.A., Irie M.,
RA   Miura T., Ohara K., Koyano H.;
RT   "Design and evaluation of azaindole-substituted N-hydroxypyridones as
RT   glyoxalase I inhibitors.";
RL   Bioorg. Med. Chem. Lett. 22:7486-7489(2012).
CC   -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC       methylglyoxal and glutathione, to S-lactoylglutathione. Involved
CC       in the regulation of TNF-induced transcriptional activity of NF-
CC       kappa-B. Required for normal osteoclastogenesis.
CC       {ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816,
CC       ECO:0000269|PubMed:9705294}.
CC   -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC       methylglyoxal. {ECO:0000269|PubMed:23122816,
CC       ECO:0000269|PubMed:9705294}.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. In the homodimer, two zinc
CC       ions are bound between subunits. {ECO:0000269|PubMed:23122816,
CC       ECO:0000269|PubMed:9705294}.
CC   -!- ENZYME REGULATION: Regulated by oxidation of Cys-139 in response
CC       to the redox state of the cell. Results in the alternative
CC       formation of cystine or glutathione-bound cysteine, the latter
CC       modification leading to reduced enzyme activity.
CC       {ECO:0000269|PubMed:20454679}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.3 mM for methylglyoxal/glutathione (native form)
CC         {ECO:0000269|PubMed:20454679};
CC         KM=0.7 mM for methylglyoxal/glutathione (reduced form)
CC         {ECO:0000269|PubMed:20454679};
CC         Vmax=0.335 umol/min/mg enzyme with methylglyoxal/glutathione as
CC         substrate (native form) {ECO:0000269|PubMed:20454679};
CC         Vmax=0.7 umol/min/mg enzyme with methylglyoxal/glutathione as
CC         substrate (reduced form) {ECO:0000269|PubMed:20454679};
CC         Note=Reduction of GLO1 was carried out by incubation with 20 mM
CC         betamercaptoethanol prior to kinetic analysis.;
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC       degradation; (R)-lactate from methylglyoxal: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23122816,
CC       ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q04760-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q04760-2; Sequence=VSP_041632;
CC         Note=No experimental confirmation available.;
CC   -!- PTM: Glutathionylation at Cys-139 inhibits enzyme activity.
CC       {ECO:0000269|PubMed:20454679}.
CC   -!- PTM: Phosphorylated at Thr-107 in the presence of CaMK2. However,
CC       this is a consensus site for phosphorylation by CK2 so
CC       phosphorylation may be mediated by CK2 rather than CaMK2.
CC       Phosphorylation is induced by TNF and suppresses the TNF-induced
CC       transcriptional activity of NF-kappa-B.
CC       {ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007}.
CC   -!- PTM: Exists in a nitric oxide (NO)-modified form. The exact nature
CC       of the modification is unknown, but it suppresses the TNF-induced
CC       transcriptional activity of NF-kappa-B.
CC   -!- MASS SPECTROMETRY: Mass=20687.4; Method=Electrospray; Range=2-184
CC       (Q04760-1); Note=Variant Glu-111.;
CC       Evidence={ECO:0000269|PubMed:20454679};
CC   -!- MASS SPECTROMETRY: Mass=20629.7; Method=Electrospray; Range=2-184
CC       (Q04760-1); Note=Variant Ala-111.;
CC       Evidence={ECO:0000269|PubMed:20454679};
CC   -!- POLYMORPHISM: Exists in three separable isoforms which originate
CC       from two alleles in the genome. These correspond to two homodimers
CC       and one heterodimer composed of two subunits showing different
CC       electrophoretic properties.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93038.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; D13315; BAA02572.1; -; mRNA.
DR   EMBL; L07837; AAA52565.1; -; mRNA.
DR   EMBL; S83285; AAB49495.1; -; mRNA.
DR   EMBL; AF146651; AAD38008.1; -; Genomic_DNA.
DR   EMBL; AB209801; BAD93038.1; ALT_INIT; mRNA.
DR   EMBL; AK293345; BAG56861.1; -; mRNA.
DR   EMBL; AK312662; BAG35544.1; -; mRNA.
DR   EMBL; BT019987; AAV38790.1; -; mRNA.
DR   EMBL; BT019988; AAV38791.1; -; mRNA.
DR   EMBL; AL391415; CAI21586.1; -; Genomic_DNA.
DR   EMBL; BC001741; AAH01741.1; -; mRNA.
DR   EMBL; BC011365; AAH11365.1; -; mRNA.
DR   EMBL; BC015934; AAH15934.1; -; mRNA.
DR   CCDS; CCDS4837.1; -. [Q04760-1]
DR   PIR; A46714; A46714.
DR   PIR; S63603; S63603.
DR   RefSeq; NP_006699.2; NM_006708.2. [Q04760-1]
DR   UniGene; Hs.268849; -.
DR   PDB; 1BH5; X-ray; 2.20 A; A/B/C/D=2-184.
DR   PDB; 1FRO; X-ray; 2.20 A; A/B/C/D=2-184.
DR   PDB; 1QIN; X-ray; 2.00 A; A/B=2-184.
DR   PDB; 1QIP; X-ray; 1.72 A; A/B/C/D=2-184.
DR   PDB; 3VW9; X-ray; 1.47 A; A/B=1-184.
DR   PDB; 3W0T; X-ray; 1.35 A; A/B/C/D=1-184.
DR   PDB; 3W0U; X-ray; 1.70 A; A/B=1-184.
DR   PDBsum; 1BH5; -.
DR   PDBsum; 1FRO; -.
DR   PDBsum; 1QIN; -.
DR   PDBsum; 1QIP; -.
DR   PDBsum; 3VW9; -.
DR   PDBsum; 3W0T; -.
DR   PDBsum; 3W0U; -.
DR   ProteinModelPortal; Q04760; -.
DR   SMR; Q04760; 3-184.
DR   BioGrid; 109001; 10.
DR   IntAct; Q04760; 3.
DR   STRING; 9606.ENSP00000362463; -.
DR   BindingDB; Q04760; -.
DR   ChEMBL; CHEMBL2424; -.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB00328; Indomethacin.
DR   PhosphoSite; Q04760; -.
DR   DMDM; 134039205; -.
DR   OGP; Q04760; -.
DR   REPRODUCTION-2DPAGE; IPI00220766; -.
DR   REPRODUCTION-2DPAGE; Q04760; -.
DR   MaxQB; Q04760; -.
DR   PaxDb; Q04760; -.
DR   PRIDE; Q04760; -.
DR   DNASU; 2739; -.
DR   Ensembl; ENST00000373365; ENSP00000362463; ENSG00000124767. [Q04760-1]
DR   GeneID; 2739; -.
DR   KEGG; hsa:2739; -.
DR   UCSC; uc003ooc.3; human. [Q04760-1]
DR   CTD; 2739; -.
DR   GeneCards; GC06M038643; -.
DR   HGNC; HGNC:4323; GLO1.
DR   HPA; CAB040541; -.
DR   HPA; CAB040542; -.
DR   MIM; 138750; gene.
DR   neXtProt; NX_Q04760; -.
DR   PharmGKB; PA28724; -.
DR   eggNOG; COG0346; -.
DR   HOVERGEN; HBG025852; -.
DR   InParanoid; Q04760; -.
DR   KO; K01759; -.
DR   OMA; WALSRKA; -.
DR   OrthoDB; EOG7XPZ6W; -.
DR   PhylomeDB; Q04760; -.
DR   TreeFam; TF105011; -.
DR   BRENDA; 4.4.1.5; 2681.
DR   SABIO-RK; Q04760; -.
DR   UniPathway; UPA00619; UER00675.
DR   EvolutionaryTrace; Q04760; -.
DR   GeneWiki; GLO1; -.
DR   GeneWiki; Lactoylglutathione_lyase; -.
DR   GenomeRNAi; 2739; -.
DR   NextBio; 10796; -.
DR   PRO; PR:Q04760; -.
DR   Bgee; Q04760; -.
DR   CleanEx; HS_GLO1; -.
DR   ExpressionAtlas; Q04760; baseline and differential.
DR   Genevestigator; Q04760; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0009438; P:methylglyoxal metabolic process; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR004361; Glyoxalase_1.
DR   InterPro; IPR018146; Glyoxalase_1_CS.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   TIGRFAMs; TIGR00068; glyox_I; 1.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR   PROSITE; PS00935; GLYOXALASE_I_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glutathionylation; Lyase;
KW   Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:20454679}.
FT   CHAIN         2    184       Lactoylglutathione lyase.
FT                                /FTId=PRO_0000168076.
FT   REGION      157    158       Substrate binding.
FT   ACT_SITE    173    173       Proton donor/acceptor.
FT                                {ECO:0000269|PubMed:10521255,
FT                                ECO:0000269|PubMed:9705294}.
FT   METAL        34     34       Zinc; shared with dimeric partner.
FT                                {ECO:0000269|PubMed:23122816,
FT                                ECO:0000269|PubMed:9218781,
FT                                ECO:0000269|PubMed:9705294}.
FT   METAL       100    100       Zinc; shared with dimeric partner.
FT                                {ECO:0000269|PubMed:23122816,
FT                                ECO:0000269|PubMed:9218781,
FT                                ECO:0000269|PubMed:9705294}.
FT   METAL       127    127       Zinc; via tele nitrogen.
FT                                {ECO:0000269|PubMed:23122816,
FT                                ECO:0000269|PubMed:9218781,
FT                                ECO:0000269|PubMed:9705294}.
FT   METAL       173    173       Zinc. {ECO:0000269|PubMed:23122816,
FT                                ECO:0000269|PubMed:9218781,
FT                                ECO:0000269|PubMed:9705294}.
FT   BINDING      34     34       Substrate; shared with dimeric partner.
FT   BINDING      38     38       Substrate; shared with dimeric partner.
FT   BINDING     104    104       Substrate; shared with dimeric partner.
FT   BINDING     123    123       Substrate.
FT   BINDING     127    127       Substrate.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:20454679}.
FT   MOD_RES      88     88       N6-succinyllysine. {ECO:0000250}.
FT   MOD_RES     107    107       Phosphothreonine.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MOD_RES     139    139       S-glutathionyl cysteine; alternate.
FT                                {ECO:0000269|PubMed:20454679}.
FT   MOD_RES     148    148       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES     148    148       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   DISULFID     19     20       {ECO:0000269|PubMed:20454679}.
FT   DISULFID     61    139       Alternate. {ECO:0000269|PubMed:20454679}.
FT   VAR_SEQ     105    119       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_041632.
FT   VARIANT      19     19       C -> Y (in dbSNP:rs17855424).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_031078.
FT   VARIANT     111    111       E -> A (in dbSNP:rs4746).
FT                                {ECO:0000269|PubMed:10564821,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7684374,
FT                                ECO:0000269|PubMed:8449929}.
FT                                /FTId=VAR_013481.
FT   MUTAGEN      19     19       C->A: No effect on NO-mediated
FT                                modification. Impaired NO-mediated
FT                                modification; when associated with A-20.
FT                                Loss of NO-mediated modification; when
FT                                associated with A-139.
FT                                {ECO:0000269|PubMed:17576200,
FT                                ECO:0000269|PubMed:19199007}.
FT   MUTAGEN      20     20       C->A: No effect on NO-mediated
FT                                modification. Impaired NO-mediated
FT                                modification; when associated with A-19.
FT                                Loss of NO-mediated modification; when
FT                                associated with A-139.
FT                                {ECO:0000269|PubMed:17576200,
FT                                ECO:0000269|PubMed:19199007}.
FT   MUTAGEN      34     34       Q->E: Reduces enzyme activity by 99%.
FT                                {ECO:0000269|PubMed:9705294}.
FT   MUTAGEN      45     45       S->A: No effect on phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN      61     61       C->A: No effect on NO-mediated
FT                                modification.
FT                                {ECO:0000269|PubMed:17576200}.
FT   MUTAGEN      69     69       S->A: No effect on phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN      94     94       S->A: No effect on phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN      98     98       T->A: No effect on phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN     100    100       E->Q: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:9705294}.
FT   MUTAGEN     102    102       T->A: No effect on phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN     107    107       T->A: Loss of phosphorylation.
FT                                {ECO:0000269|PubMed:19199007}.
FT   MUTAGEN     139    139       C->A: Impaired NO-mediated modification.
FT                                Loss of NO-mediated modification; when
FT                                associated with A-19 or A-20.
FT                                {ECO:0000269|PubMed:17576200,
FT                                ECO:0000269|PubMed:19199007}.
FT   MUTAGEN     173    173       E->Q: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:9705294}.
FT   HELIX        13     18
FT   HELIX        25     27
FT   STRAND       31     38
FT   HELIX        42     51
FT   STRAND       56     63
FT   TURN         64     67
FT   STRAND       68     75
FT   HELIX        78     80
FT   HELIX        85     92
FT   STRAND       95    104
FT   HELIX       107    109
FT   STRAND      118    122
FT   STRAND      124    131
FT   HELIX       135    144
FT   STRAND      149    151
FT   STRAND      155    158
FT   STRAND      162    165
FT   STRAND      171    175
FT   HELIX       177    179
FT   HELIX       181    183
SQ   SEQUENCE   184 AA;  20778 MW;  46291B7878070028 CRC64;
     MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK
     CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS
     DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM
     ATLM
//
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