ID F2L973_BURGS Unreviewed; 408 AA.
AC F2L973;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN OrderedLocusNames=bgla_1g06560 {ECO:0000313|EMBL:AEA59348.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA59348.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA59348.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA59348.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(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};
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DR EMBL; CP002599; AEA59348.1; -; Genomic_DNA.
DR RefSeq; WP_013696704.1; NC_015381.1.
DR AlphaFoldDB; F2L973; -.
DR STRING; 999541.bgla_1g06560; -.
DR KEGG; bgd:bgla_1g06560; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_4; -.
DR Proteomes; UP000008316; Chromosome 1.
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: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}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 16..47
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 66..89
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 408 AA; 45152 MW; B0AC2D144962E2EF CRC64;
MQTKLADFIR DTPDGAEAES ILRKCVHCGF CTATCPTYQL LGDELDGPRG RIYLIKQMLE
GAPVTRSTQQ HLDRCLTCRS CESTCPSGVQ YGRLVEIGRQ QLETRVPRTL SQRLMRRALA
SFVPNGALFA PAMRIGQQVR PLLPKRLRDK VPPRTRPLAW PTARHERRML MLAGCVQPSM
MPNINVATAR VLDALGIETM IAPEAGCCGA IRLHLNYRDE ALADARRNID AWWPHIEAGA
EAIVMNASGC GATVLEYAHL LRDDPAYADK ARRVVELTRD VSELLAGFET RLVALAKRRG
MQTVAYHPPC TLQHGQQSRG KVERLLEALG VELRVPADSH LCCGSAGTYS LTQPSLSYKL
RKQKLARLAE LDPQLIVSGN IGCLAHLQSG TATPVMHWIQ LVEQLLDD
//
