ID A0A3Q9QU54_9BACI Unreviewed; 447 AA.
AC A0A3Q9QU54;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=CHR53_14185 {ECO:0000313|EMBL:AZU62340.1};
OS Neobacillus mesonae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU62340.1, ECO:0000313|Proteomes:UP000282892};
RN [1] {ECO:0000313|EMBL:AZU62340.1, ECO:0000313|Proteomes:UP000282892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H20-5 {ECO:0000313|EMBL:AZU62340.1,
RC ECO:0000313|Proteomes:UP000282892};
RA Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT efficient strain improving plant abiotic stress resistance.";
RL Submitted (JUL-2017) 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; CP022572; AZU62340.1; -; Genomic_DNA.
DR RefSeq; WP_066399448.1; NZ_KV440949.1.
DR AlphaFoldDB; A0A3Q9QU54; -.
DR STRING; 1193713.GCA_001636315_05279; -.
DR KEGG; nmk:CHR53_14185; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000282892; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282892};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 10..39
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 61..85
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 447 AA; 49793 MW; 881DCDB84C6A8164 CRC64;
MIQDLELIKK EIKYDKTLNC VQCGYCLPVC PTYITMGKET HSPRGRINLV KMVGEGKMTD
LSIMEEPMDL CLGCRACETA CPTGVQYGEI LEGARSVMKK SKKSPMLQTI LLSKVIPSHK
MMEQAGNAFW LYEKSGMQTM LRKSGLLDKL PAHLGTFESI IPAAVSPKER ARFPKRVQME
SPGVMAQTGT DQNGEKREKK YTVAFFTGCI MDAMFRRINQ LSVELLAKAG CEVVMMENQT
CCGALHAHTG DMKESKKLAK QNIAAFEKEN VDFIVNNAGG CGAMLKEYDR LLEDEPEWLE
RAKEFTEKNK DISEVLVLCG GIPVINHPPE KVTYQRSCHM TNVQKVKIEP VQLIKSIPNV
ELIEMNEGDM CCGSAGIYNI VNYEASMEIL DRKMGNVKDT LATTILTTNP GCLLQMKLGV
KREGLTQKVR VLHLVEFLAE AAGVSSW
//
