ID A0A1M4YV99_9FIRM Unreviewed; 399 AA.
AC A0A1M4YV99;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=SAMN02745218_01427 {ECO:0000313|EMBL:SHF09675.1};
OS Desulfofundulus australicus DSM 11792.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofundulus.
OX NCBI_TaxID=1121425 {ECO:0000313|EMBL:SHF09675.1, ECO:0000313|Proteomes:UP000184196};
RN [1] {ECO:0000313|EMBL:SHF09675.1, ECO:0000313|Proteomes:UP000184196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11792 {ECO:0000313|EMBL:SHF09675.1,
RC ECO:0000313|Proteomes:UP000184196};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQUW01000015; SHF09675.1; -; Genomic_DNA.
DR RefSeq; WP_073164582.1; NZ_FQUW01000015.1.
DR AlphaFoldDB; A0A1M4YV99; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000184196; 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; 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..34
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 57..85
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 399 AA; 43413 MW; 487994ED5F5D2310 CRC64;
MLENNEEVRY QVNRCSRCGS CREVCPVFLQ AGSEPWVARA RVQLAGAALE GQLPFSRRFG
EIMDACLLCR ACVAHCPNGV RVDELVLWAR AEAVRRKGLS PARMVLLRGA LPSRRKLALI
SRMAALCQRA SILKNFRGMK LPAFHTLPFT HLYRPAGLKK PSFTVAYFVG CMTQYVYHQS
GRAVLKVLEQ NNVQVLLAGS GCCGMPALAA GDLKTARLLA RRNVENFKKL GADFVVTDCA
TCGEMLKLYG RLLGDEEAGE LAARVQDITF FLVHTGGFHE GKVRVPLVVT YHDPCHLKRG
QGVYLEPRKI LAGIAGLTLV EMPRSDACCG LAGSFGFTHR ELSQKILRAK IENIRATGAQ
AVVTGCPSCR LQLASGLAGE GAALPVFHTV ELLALSYGG
//
