ID GALM_HUMAN Reviewed; 342 AA.
AC Q96C23; Q53RY1; Q8NIA2; V9HWA8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Galactose mutarotase {ECO:0000303|PubMed:12753898, ECO:0000303|PubMed:15026423};
DE EC=5.1.3.3 {ECO:0000269|PubMed:12753898};
DE AltName: Full=Aldose 1-epimerase {ECO:0000303|PubMed:12753898};
GN Name=GALM {ECO:0000312|HGNC:HGNC:24063}; ORFNames=BLOCK25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gorry M.C., Zhang Y., Marks J.J., Suppes B., Hart P.S., Cortelli J.R.,
RA Pallos D., Hart T.C.;
RT "Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li J.Y., Wang H.Y., Liu F.J., Liu J.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, MUTAGENESIS OF HIS-107; HIS-176 AND GLU-307, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RX PubMed=12753898; DOI=10.1016/s0014-5793(03)00364-8;
RA Timson D.J., Reece R.J.;
RT "Identification and characterisation of human aldose 1-epimerase.";
RL FEBS Lett. 543:21-24(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
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., Buerckstuemmer T.,
RA 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12] {ECO:0007744|PDB:1SNZ, ECO:0007744|PDB:1SO0}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH BETA-D-GALACTOSE,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=15026423; DOI=10.1074/jbc.m402347200;
RA Thoden J.B., Timson D.J., Reece R.J., Holden H.M.;
RT "Molecular structure of human galactose mutarotase.";
RL J. Biol. Chem. 279:23431-23437(2004).
RN [13]
RP VARIANTS GALAC4 82-ARG--ALA-342 DEL; ARG-142; GLY-267 AND 311-TRP--ALA-342
RP DEL, CHARACTERIZATION OF VARIANTS GALAC4 82-ARG--ALA-342 DEL; ARG-142;
RP GLY-267 AND 311-TRP--ALA-342 DEL, FUNCTION, AND INVOLVEMENT IN GALAC4.
RX PubMed=30451973; DOI=10.1038/s41436-018-0340-x;
RA Wada Y., Kikuchi A., Arai-Ichinoi N., Sakamoto O., Takezawa Y., Iwasawa S.,
RA Niihori T., Nyuzuki H., Nakajima Y., Ogawa E., Ishige M., Hirai H.,
RA Sasai H., Fujiki R., Shirota M., Funayama R., Yamamoto M., Ito T.,
RA Ohara O., Nakayama K., Aoki Y., Koshiba S., Fukao T., Kure S.;
RT "Biallelic GALM pathogenic variants cause a novel type of galactosemia.";
RL Genet. Med. 21:1286-1294(2019).
CC -!- FUNCTION: Mutarotase that catalyzes the interconversion of beta-D-
CC galactose and alpha-D-galactose during galactose metabolism
CC (PubMed:12753898). Beta-D-galactose is metabolized in the liver into
CC glucose 1-phosphate, the primary metabolic fuel, by the action of four
CC enzymes that constitute the Leloir pathway: GALM, GALK1
CC (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and
CC GALE (UDP-galactose-4'-epimerase) (PubMed:30451973). Involved in the
CC maintenance of the equilibrium between the beta- and alpha-anomers of
CC galactose, therefore ensuring a sufficient supply of the alpha-anomer
CC for GALK1 (PubMed:12753898). Also active on D-glucose although shows a
CC preference for galactose over glucose (PubMed:12753898).
CC {ECO:0000269|PubMed:12753898, ECO:0000269|PubMed:30451973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose = beta-D-galactose; Xref=Rhea:RHEA:28675,
CC ChEBI:CHEBI:27667, ChEBI:CHEBI:28061; EC=5.1.3.3;
CC Evidence={ECO:0000269|PubMed:12753898};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28677;
CC Evidence={ECO:0000305|PubMed:12753898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC Evidence={ECO:0000269|PubMed:12753898};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 mM for galactose (at 20 degrees Celsius)
CC {ECO:0000269|PubMed:12753898};
CC KM=54 mM for glucose (at 20 degrees Celsius)
CC {ECO:0000269|PubMed:12753898};
CC Note=kcat is 12000 sec(-1) with galactose as substrate
CC (PubMed:12753898). kcat is 4900 sec(-1) with glucose as substrate
CC (PubMed:12753898). {ECO:0000269|PubMed:12753898};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:12753898}.
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000305|PubMed:12753898}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12753898,
CC ECO:0000269|PubMed:15026423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISEASE: Galactosemia 4 (GALAC4) [MIM:618881]: A form of galactosemia,
CC an inborn error of galactose metabolism typically manifesting in the
CC neonatal period, after ingestion of galactose, with jaundice,
CC hepatosplenomegaly, hepatocellular insufficiency, food intolerance,
CC hypoglycemia, renal tubular dysfunction, muscle hypotonia, sepsis and
CC cataract. GALAC4 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:30451973}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL62475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY064382; AAL62475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY064381; AAL62475.1; JOINED; Genomic_DNA.
DR EMBL; AY064379; AAL62475.1; JOINED; Genomic_DNA.
DR EMBL; AY064380; AAL62475.1; JOINED; Genomic_DNA.
DR EMBL; AY064378; AAL62475.1; JOINED; Genomic_DNA.
DR EMBL; AY064385; AAL62476.1; -; Genomic_DNA.
DR EMBL; AY064378; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; AY064380; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; AY064379; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; AY064381; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; AY064384; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; AY064383; AAL62476.1; JOINED; Genomic_DNA.
DR EMBL; EU794611; ACJ13665.1; -; mRNA.
DR EMBL; AK291489; BAF84178.1; -; mRNA.
DR EMBL; AC074366; AAX93101.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00367.1; -; Genomic_DNA.
DR EMBL; BC014916; AAH14916.1; -; mRNA.
DR EMBL; BC019263; AAH19263.1; -; mRNA.
DR CCDS; CCDS1797.1; -.
DR RefSeq; NP_620156.1; NM_138801.2.
DR RefSeq; XP_011530842.1; XM_011532540.1.
DR PDB; 1SNZ; X-ray; 2.20 A; A/B=1-342.
DR PDB; 1SO0; X-ray; 2.30 A; A/B/C/D=1-342.
DR PDBsum; 1SNZ; -.
DR PDBsum; 1SO0; -.
DR AlphaFoldDB; Q96C23; -.
DR SMR; Q96C23; -.
DR BioGRID; 126244; 23.
DR IntAct; Q96C23; 3.
DR STRING; 9606.ENSP00000272252; -.
DR iPTMnet; Q96C23; -.
DR PhosphoSitePlus; Q96C23; -.
DR BioMuta; GALM; -.
DR DMDM; 67463772; -.
DR EPD; Q96C23; -.
DR jPOST; Q96C23; -.
DR MassIVE; Q96C23; -.
DR MaxQB; Q96C23; -.
DR PaxDb; 9606-ENSP00000272252; -.
DR PeptideAtlas; Q96C23; -.
DR ProteomicsDB; 76151; -.
DR Pumba; Q96C23; -.
DR Antibodypedia; 29513; 279 antibodies from 26 providers.
DR DNASU; 130589; -.
DR Ensembl; ENST00000272252.10; ENSP00000272252.5; ENSG00000143891.17.
DR GeneID; 130589; -.
DR KEGG; hsa:130589; -.
DR MANE-Select; ENST00000272252.10; ENSP00000272252.5; NM_138801.3; NP_620156.1.
DR UCSC; uc002rqy.4; human.
DR AGR; HGNC:24063; -.
DR CTD; 130589; -.
DR DisGeNET; 130589; -.
DR GeneCards; GALM; -.
DR HGNC; HGNC:24063; GALM.
DR HPA; ENSG00000143891; Tissue enhanced (adrenal gland, kidney).
DR MalaCards; GALM; -.
DR MIM; 137030; gene.
DR MIM; 618881; phenotype.
DR neXtProt; NX_Q96C23; -.
DR OpenTargets; ENSG00000143891; -.
DR Orphanet; 570422; Galactose mutarotase deficiency.
DR PharmGKB; PA134980075; -.
DR VEuPathDB; HostDB:ENSG00000143891; -.
DR eggNOG; KOG1604; Eukaryota.
DR GeneTree; ENSGT00510000047589; -.
DR HOGENOM; CLU_031753_2_0_1; -.
DR InParanoid; Q96C23; -.
DR OMA; AFCCEPG; -.
DR OrthoDB; 118242at2759; -.
DR PhylomeDB; Q96C23; -.
DR TreeFam; TF324207; -.
DR BioCyc; MetaCyc:HS07125-MONOMER; -.
DR BRENDA; 5.1.3.3; 2681.
DR PathwayCommons; Q96C23; -.
DR SABIO-RK; Q96C23; -.
DR SignaLink; Q96C23; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 130589; 12 hits in 1158 CRISPR screens.
DR ChiTaRS; GALM; human.
DR EvolutionaryTrace; Q96C23; -.
DR GeneWiki; Galactose_mutarotase; -.
DR GenomeRNAi; 130589; -.
DR Pharos; Q96C23; Tbio.
DR PRO; PR:Q96C23; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96C23; Protein.
DR Bgee; ENSG00000143891; Expressed in kidney epithelium and 189 other cell types or tissues.
DR ExpressionAtlas; Q96C23; baseline and differential.
DR Genevisible; Q96C23; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:MGI.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IDA:MGI.
DR GO; GO:0006012; P:galactose metabolic process; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR CDD; cd09019; galactose_mutarotase_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
DR InterPro; IPR015443; Aldose_1-epimerase.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR047215; Galactose_mutarotase-like.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1.
DR PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Cytoplasm;
KW Disease variant; Isomerase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..342
FT /note="Galactose mutarotase"
FT /id="PRO_0000197433"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15026423"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15026423"
FT BINDING 81..82
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT BINDING 107
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT BINDING 176..178
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT BINDING 243
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT BINDING 279
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT BINDING 307
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:15026423,
FT ECO:0007744|PDB:1SO0"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HG4"
FT VARIANT 82..342
FT /note="Missing (in GALAC4; loss of protein accumulation)"
FT /evidence="ECO:0000269|PubMed:30451973"
FT /id="VAR_083547"
FT VARIANT 142
FT /note="G -> R (in GALAC4; uncertain significance; decreased
FT protein stability; dbSNP:rs114440198)"
FT /evidence="ECO:0000269|PubMed:30451973"
FT /id="VAR_083548"
FT VARIANT 190
FT /note="N -> Y (in dbSNP:rs6741892)"
FT /id="VAR_024451"
FT VARIANT 267
FT /note="R -> G (in GALAC4; decreased protein stability)"
FT /evidence="ECO:0000269|PubMed:30451973"
FT /id="VAR_083549"
FT VARIANT 311..342
FT /note="Missing (in GALAC4; decreased protein stability)"
FT /evidence="ECO:0000269|PubMed:30451973"
FT /id="VAR_083550"
FT MUTAGEN 107
FT /note="H->A: Decreased activity by 5-fold."
FT /evidence="ECO:0000269|PubMed:12753898"
FT MUTAGEN 176
FT /note="H->A: Decreased activity by 300-fold."
FT /evidence="ECO:0000269|PubMed:12753898"
FT MUTAGEN 307
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12753898"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1SNZ"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 156..167
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1SO0"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:1SNZ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 267..281
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1SNZ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:1SNZ"
FT STRAND 331..341
FT /evidence="ECO:0007829|PDB:1SNZ"
SQ SEQUENCE 342 AA; 37766 MW; 611A54AE7E85813E CRC64;
MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA
ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP
RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN
LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN
GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK
HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA
//
