ID F7QRH8_9BRAD Unreviewed; 433 AA.
AC F7QRH8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=CSIRO_4199 {ECO:0000313|EMBL:EGP06189.1};
OS Bradyrhizobiaceae bacterium SG-6C.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP06189.1, ECO:0000313|Proteomes:UP000003148};
RN [1] {ECO:0000313|EMBL:EGP06189.1, ECO:0000313|Proteomes:UP000003148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP06189.1,
RC ECO:0000313|Proteomes:UP000003148};
RX PubMed=21742875; DOI=10.1128/JB.05647-11;
RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA Pandey G.;
RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT Bradyrhizobiaceae Strain SG-6C.";
RL J. Bacteriol. 193:5057-5057(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:EGP06189.1}.
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DR EMBL; AFOF01000037; EGP06189.1; -; Genomic_DNA.
DR AlphaFoldDB; F7QRH8; -.
DR STRING; 709797.CSIRO_4199; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_5; -.
DR Proteomes; UP000003148; Chromosome.
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:UniProtKB-EC.
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; 1.
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:EGP06189.1};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 16..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 433 AA; 47205 MW; 35751908B2E2D587 CRC64;
MQTNFSLVAL AESHMRESEK ILRACVHCGF CTATCPTYLL LGDELDSPRG RIYLIKDMFE
NEKPASEKVV KHIDRCLSCL SCMTTCPSGV HYMHLVDHAR AHITETYKRP LIDRVLRSAL
AAVLPNPKWL RPALFAASVV RPIKKWLVRL PGGTQLGAMI DLAPALRPRK HAPPELNEGN
RRGRVAILTG CAQQVIAPGI NDAAIRLLRR HGIEVTSPRG EGCCGALVHH MGYEDSALDA
ARRNVDVWTR ELDENGLDAI IVTASGCGTT VKDYGFMLRE DKAYASKAAR VSELAQDISE
YLHTLRLQGP TRATGQLVAY HSACSMQHGQ RIVDQPKSLL TQMGFVVSDV PEGHICCGSA
GTYNVLQPEI AGQLRSRKVA NIEKLKPQII ASGNLGCITQ IGAGTAIPIV HTVELLDWAT
GGPLPDAMEG NFD
//
