ID H0SX51_9BRAD Unreviewed; 439 AA.
AC H0SX51;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=glcF {ECO:0000313|EMBL:CCD98778.1};
GN ORFNames=BRAS3809_2210002 {ECO:0000313|EMBL:CCD98778.1};
OS Bradyrhizobium sp. STM 3809.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCD98778.1, ECO:0000313|Proteomes:UP000004098};
RN [1] {ECO:0000313|Proteomes:UP000004098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCD98778.1}.
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DR EMBL; CAFJ01000137; CCD98778.1; -; Genomic_DNA.
DR RefSeq; WP_008961379.1; NZ_CAFJ01000137.1.
DR AlphaFoldDB; H0SX51; -.
DR OrthoDB; 9765258at2; -.
DR Proteomes; UP000004098; Unassembled WGS sequence.
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; SSF54862; 4Fe-4S ferredoxins; 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:CCD98778.1};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 13..45
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 67..96
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 439 AA; 47007 MW; 8F30952BDC0B6516 CRC64;
MKTEFTLAQL ADPDIAVADK ILRACVHCGF CTATCPTYVL LGDELDSPRG RIYLIKQMLE
KEQAPTPDVV KHIDRCLSCL SCMTTCPSGV HYMHLVDQAR VRIEETYQRP LTDRLLRAVL
AHVLPRPQLF RLAMTLARLG RPFKALLPAS SSSTPTPSLW RRLRAMLDLA PAAALPPPGP
AGGSVFAAQG ARRGRVALLQ GCAQAALAPR INQAAINVLT RHGIEVVLVK DEQCCGALTH
HMGQDDDAMA RARANVGVWT AEAARGGLDA ILVTTSGCGT VIKDYGHMLR EDPHYAAPAA
AVSAMAKDIS EYLAGLELKV TAETRGLNVA YHSACSLQHG QKITSIPKEL LSKSGFVVKD
IPESHLCCGS AGTYNILQPD IAMRLRDRKV ANIATVKPDV IAAGNIGCMM QIASGTGIPV
VHTVELLDWA TGGPRPGLN
//
