ID A0A117SBX2_9FIRM Unreviewed; 421 AA.
AC A0A117SBX2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=APF84_10855 {ECO:0000313|EMBL:KUO63018.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO63018.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO63018.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO63018.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO63018.1}.
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DR EMBL; LOEZ01000053; KUO63018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SBX2; -.
DR STRING; 1734398.APF84_10855; -.
DR Proteomes; UP000053404; Unassembled WGS sequence.
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:SF19; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT C; 1.
DR PANTHER; PTHR32479; 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 8..38
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 59..89
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 421 AA; 46253 MW; F24311B8EE8D47D6 CRC64;
MLREELYDQV KKLIDKCNRC GFCRSVCPSL AELGWESTSP RGRVFLVGEV LAGRIPLTGD
VVSRIDQCLL CRNCMAVCPV GGKIDQVIIA FRQLAAQEMG VATSKKLMLN MLSDHRGLCD
VMAPVAAVLE HIPFKETPGG GAIFRLNKKM RLLPMFGGKP LMSQFQHIKV DKPIKKVAFY
VGCYINYMGV NVGRAVLNIL ARNGVEVVIP QTQTCCGVPF FASGMVEKAV TLVRQNIDAL
EEANVDAVIY ACGSCGTGLK EWARHPEIGS EYAEKAKKLE EKTFEIGEFL IDQLEVKELP
SLPKPTRVTY HDSCHLAVGA GVIEQPRTLL KMMGNAEYIE MPEANTCCGM GGLFSVNHYD
LSRKINSRKI DKIMSVNPQV VTSGCPGCNL HIMDGLNKAG SDIVTSHYIE LINNAYDCAQ
E
//
