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Database: UniProt
Entry: K1R647_CRAGI
LinkDB: K1R647_CRAGI
Original site: K1R647_CRAGI 
ID   K1R647_CRAGI            Unreviewed;       179 AA.
AC   K1R647;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081};
DE            EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE   AltName: Full=Aldoketomutase {ECO:0000256|ARBA:ARBA00030892};
DE   AltName: Full=Ketone-aldehyde mutase {ECO:0000256|ARBA:ARBA00030291};
DE   AltName: Full=Methylglyoxalase {ECO:0000256|ARBA:ARBA00032460};
DE   AltName: Full=S-D-lactoylglutathione methylglyoxal lyase {ECO:0000256|ARBA:ARBA00033298};
GN   ORFNames=CGI_10023831 {ECO:0000313|EMBL:EKC29441.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC29441.1};
RN   [1] {ECO:0000313|EMBL:EKC29441.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC29441.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
RN   [2] {ECO:0000313|EnsemblMetazoa:G12696.4:cds}
RP   IDENTIFICATION.
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EnsemblMetazoa:G12696.4:cds};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604361-3};
CC       Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC       bound between subunits. {ECO:0000256|PIRSR:PIRSR604361-3};
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC       (R)-lactate from methylglyoxal: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005008}.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family.
CC       {ECO:0000256|ARBA:ARBA00010363}.
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DR   EMBL; JH823229; EKC29441.1; -; Genomic_DNA.
DR   RefSeq; XP_011422530.1; XM_011424228.1.
DR   EnsemblMetazoa; G12696.4; G12696.4:cds; G12696.
DR   EnsemblMetazoa; G12696.7; G12696.7:cds; G12696.
DR   HOGENOM; CLU_046006_1_1_1; -.
DR   OMA; NWGTESY; -.
DR   OrthoDB; 245930at2759; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000005408; Unplaced.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07233; GlxI_Zn; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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   InterPro; IPR037523; VOC.
DR   NCBIfam; TIGR00068; glyox_I; 1.
DR   PANTHER; PTHR10374:SF30; LACTOYLGLUTATHIONE LYASE; 1.
DR   PANTHER; PTHR10374; LACTOYLGLUTATHIONE LYASE GLYOXALASE I; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EKC29441.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005408};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR604361-3}.
FT   DOMAIN          26..172
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   ACT_SITE        168
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         152..153
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-2"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
SQ   SEQUENCE   179 AA;  20596 MW;  6C177A1536D245EE CRC64;
     MAQTGLTNEE VAKACQQPDE ATKDFFFQQT MLRVKDPKRS LEFYTKVMGM RLLKKFDFPA
     MSFSLYFMGY DKAENIPQDE TERTRYVFQQ KATLELTHNW GTENDPEQSY HNGNSDPRGF
     GHIGIVVPDV DKACERFESL GVEFVKKPND GKMKGLAFIK DPDGYWIEIL NPINMSTIS
//
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