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Database: UniProt
Entry: Q2RMG1_MOOTA
LinkDB: Q2RMG1_MOOTA
Original site: Q2RMG1_MOOTA 
ID   Q2RMG1_MOOTA            Unreviewed;       431 AA.
AC   Q2RMG1;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   OrderedLocusNames=Moth_0039 {ECO:0000313|EMBL:ABC18378.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18378.1};
RN   [1] {ECO:0000313|EMBL:ABC18378.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC18378.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000232; ABC18378.1; -; Genomic_DNA.
DR   RefSeq; YP_428921.1; NC_007644.1.
DR   AlphaFoldDB; Q2RMG1; -.
DR   STRING; 264732.Moth_0039; -.
DR   DNASU; 3830905; -.
DR   EnsemblBacteria; ABC18378; ABC18378; Moth_0039.
DR   KEGG; mta:Moth_0039; -.
DR   PATRIC; fig|264732.11.peg.41; -.
DR   eggNOG; COG0247; Bacteria.
DR   HOGENOM; CLU_023081_0_1_9; -.
DR   OrthoDB; 5241828at2; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:SF20; 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}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          6..35
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          57..88
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   431 AA;  48009 MW;  F98E7ED51A571703 CRC64;
     MVKTFRQREE DIVRCNRCGF CEEVCPTYKA TGEEFSLARG RNRLMRQSME GKLDLTKEPE
     INQHIYSCLL CGACVAACPS SVITDTLIKT ARAEITRAKG QPFPIRMALR GVLANQRRLT
     LGAKVLRFYQ RSGARWLARH IGFLNLMGSL GKAEGLLPAI PEKTLRVQLP QLLKKPMKPR
     HKVAYFAGCM INNFFTAVGE ATLRVYQEND IEVVVPTSNC CGIPHEAYGD IEMQIKLAKE
     NLDAFSRYEV EAIVTDCASC AHGLHSYAEL LQDDPHYGPL AAQLAAKVKD ASQYLVEIGF
     KKEMGPVNAT VTYHDPCHAA RGLKVKEQPR EILKSIPGVK FVEMNESDWC CGGAGSYNVT
     HYELSRKILA RKMDNFKKTG AEYLATSCPA CLMQLAHGLD VYRLSGKAIH VMQILDQAYQ
     NRAVRSKAKA G
//
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