GenomeNet

Database: UniProt
Entry: A0A099CSZ0_9GAMM
LinkDB: A0A099CSZ0_9GAMM
Original site: A0A099CSZ0_9GAMM 
ID   A0A099CSZ0_9GAMM        Unreviewed;       404 AA.
AC   A0A099CSZ0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=HNQ86_002588 {ECO:0000313|EMBL:MBB6185243.1}, LF63_0113325
GN   {ECO:0000313|EMBL:KGI76899.1};
OS   Oleiagrimonas soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Oleiagrimonas.
OX   NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI76899.1, ECO:0000313|Proteomes:UP000029708};
RN   [1] {ECO:0000313|EMBL:KGI76899.1, ECO:0000313|Proteomes:UP000029708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3.5X {ECO:0000313|EMBL:KGI76899.1,
RC   ECO:0000313|Proteomes:UP000029708};
RA   Fang T., Wang H.;
RT   "Xanthomonadaceae 3.5X direct submission.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB6185243.1, ECO:0000313|Proteomes:UP000560000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 107085 {ECO:0000313|EMBL:MBB6185243.1,
RC   ECO:0000313|Proteomes:UP000560000};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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};
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:KGI76899.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JROI01000015; KGI76899.1; -; Genomic_DNA.
DR   EMBL; JACHET010000001; MBB6185243.1; -; Genomic_DNA.
DR   RefSeq; WP_043102584.1; NZ_KN196470.1.
DR   AlphaFoldDB; A0A099CSZ0; -.
DR   STRING; 1543381.LF63_0113325; -.
DR   HOGENOM; CLU_023081_0_1_6; -.
DR   OrthoDB; 9765258at2; -.
DR   Proteomes; UP000029708; Unassembled WGS sequence.
DR   Proteomes; UP000560000; Unassembled WGS sequence.
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:SF19; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT C; 1.
DR   PANTHER; PTHR32479; 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; SSF46548; alpha-helical ferredoxin; 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:UP000029708};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          8..39
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          62..85
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          158..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  43650 MW;  7832ACC3363D8CAA CRC64;
     MNRMFDDPHA SIAELADQCV MCGLCLPHCP TYALDGTEAE SPRGRIQLAR ALADGTLTGE
     LDAARLHLDH CLSCRQCERV CPSQVRFGEL MVRTRALIGP APQRPSRLLR LLSRPRLTQM
     IAVATRLARA PRWMPALLRR FGMARDSAML AALRMLDTSR PPRPTPRTVA PSSTQHASAR
     TRVALYPGCV ASVKDRAALE AAASLLEAAG FDVHRLPARC CGAMDRHDGL SARAANAASA
     TERAWREAGA IDTVLTVTPG CLDTLGHDLP QARVEDVLGF LARHADRLRF APLRLRVALH
     VPCSRRNGPR DEADVQTLLK RIPGLELRVL PVSAGCCGAA GSHALTFPTR AERLRALTLA
     PLADLAVDCL LSSNIGCRLH LAAGDRALPT EHPLSLLARQ LESA
//
DBGET integrated database retrieval system