ID A2SM04_METPP Unreviewed; 413 AA.
AC A2SM04;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN OrderedLocusNames=Mpe_A3640 {ECO:0000313|EMBL:ABM96593.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96593.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM96593.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC glycolate to glyoxylate. {ECO:0000256|PIRNR:PIRNR000139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655; EC=1.1.99.14;
CC Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000256|PIRNR:PIRNR000139};
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DR EMBL; CP000555; ABM96593.1; -; Genomic_DNA.
DR RefSeq; WP_011831213.1; NC_008825.1.
DR AlphaFoldDB; A2SM04; -.
DR STRING; 420662.Mpe_A3640; -.
DR KEGG; mpt:Mpe_A3640; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_4; -.
DR OMA; VYQDACH; -.
DR Proteomes; UP000000366; Chromosome.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR012257; Glc_ox_4Fe-4S.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR32479; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR32479:SF17; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR PIRSF; PIRSF000139; Glc_ox_4Fe-4S; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000139};
KW Electron transport {ECO:0000256|PIRNR:PIRNR000139};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000139};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR000139};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000139};
KW Oxidoreductase {ECO:0000313|EMBL:ABM96593.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 16..47
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 66..89
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 413 AA; 44139 MW; 2C22C498FE5B8ECA CRC64;
MQTTLAPEYQ GSADGADAEA ILRKCVHCGF CTATCPTYQL LGDELDGPRG RIYLIKQVLE
GAEPTRKTQL HLDRCLTCRN CESTCPSGVQ YGALVDIGRR VVDAKVERPA GERAARTALK
EGLTSPLFAP AMKLGQLFRP LVPTALKAKV PPKAPASAHR WPTRSHPRKV LMLLGCVQPA
MAPNINSATA RVLDAAGIQT LVADDAGCCG AIRDHLGDHE GGLADMRRNI DAWWPLVEGL
TGQGAVEAIV MNASGCGVTV KDYARHLKHD PAYAERAAKI SALTRDLSEL LPDLVPKLKP
RLRGKAPKLA FHPPCTLQHG QQLRGGIEGG LRELGFDITL TPTDSHLCCG SAGTYSVLQP
ALAYQLRDRK LAALAPVGAQ AIVSANIGCI QHLQSGTPTP VKHWVEVLDE ALA
//