ID A2BQD3_PROMS Unreviewed; 129 AA.
AC A2BQD3;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537};
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 Name=gloA {ECO:0000313|EMBL:ABM69994.1};
GN OrderedLocusNames=A9601_07081 {ECO:0000313|EMBL:ABM69994.1};
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=146891 {ECO:0000313|EMBL:ABM69994.1, ECO:0000313|Proteomes:UP000002590};
RN [1] {ECO:0000313|EMBL:ABM69994.1, ECO:0000313|Proteomes:UP000002590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601 {ECO:0000313|EMBL:ABM69994.1,
RC ECO:0000313|Proteomes:UP000002590};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000817};
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; CP000551; ABM69994.1; -; Genomic_DNA.
DR RefSeq; WP_011818156.1; NC_008816.1.
DR AlphaFoldDB; A2BQD3; -.
DR STRING; 146891.A9601_07081; -.
DR KEGG; pmb:A9601_07081; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_1_3; -.
DR OrthoDB; 192739at2; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000002590; Chromosome.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR46036:SF5; LACTOYLGLUTATHIONE LYASE; 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:ABM69994.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 2..128
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 56
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 76
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 124
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 129 AA; 14818 MW; 10FBF8D52B6EF064 CRC64;
MRILHTMLRV GDLDKSIDFY VNRLGMNLLR KKDYPHGKFT LAFVGYGSEK ENSVIELTYN
WDKKSEDYEL GDKYGHIAIG VKDIHLICQG LENNGCKITT KPKTMKNSTT VLAFVEDPDG
YKIELIERD
//
