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Database: UniProt
Entry: A2SM04_METPP
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Original site: A2SM04_METPP 
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
//
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