ID A0A0H3KCE3_BURM1 Unreviewed; 408 AA.
AC A0A0H3KCE3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=glcD {ECO:0000313|EMBL:BAG42548.1};
GN OrderedLocusNames=BMULJ_00584 {ECO:0000313|EMBL:BAG42548.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG42548.1, ECO:0000313|Proteomes:UP000008815};
RN [1] {ECO:0000313|EMBL:BAG42548.1, ECO:0000313|Proteomes:UP000008815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; AP009385; BAG42548.1; -; Genomic_DNA.
DR RefSeq; WP_006412284.1; NC_010804.1.
DR AlphaFoldDB; A0A0H3KCE3; -.
DR STRING; 395019.BMULJ_00584; -.
DR KEGG; bmj:BMULJ_00584; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_4; -.
DR Proteomes; UP000008815; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:BAG42548.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008815};
KW 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; 45408 MW; 9D1AEB058AE55CDC CRC64;
MQTNLADFIR DTPDGNEADA ILRKCVHCGF CTATCPTYQL LGDELDGPRG RIYLIKQMVE
GAKVTRSTQQ HLDRCLTCRS CETTCPSGVQ YGRLVEIGRK HVEAQVQRPL SQRLVRRLLA
SLVPNATLFS PVMRLGQHVR PLLPKRLRDK VPPRTRLLEW PQRTHPRKML MLGGCVQPSM
LPNINIATAR VLDALGVETI VAPDAGCCGA IRLHLNYHDE ALDDARRNID AWWPYVEQGV
EAIVMNASGC GATVLEYAHL LRDDPAYAEK ARRIVALTRD ISDVLLAFEA ELATLGRRRA
IHTVAYHPPC TLQHGQQSRG KVERLLETLG IDVRLPADSH LCCGSAGTYS LTQPSLSYRL
RKQKLLKLQA LEPQMIVSGN VGCIAHLQSG TQIPVAHWIQ LVEHLIYG
//
