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Database: UniProt
Entry: A0A0S2THK7_9GAMM
LinkDB: A0A0S2THK7_9GAMM
Original site: A0A0S2THK7_9GAMM 
ID   A0A0S2THK7_9GAMM        Unreviewed;       408 AA.
AC   A0A0S2THK7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=Tel_16460 {ECO:0000313|EMBL:ALP54616.1};
OS   Candidatus Tenderia electrophaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Candidatus Tenderia.
OX   NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP54616.1, ECO:0000313|Proteomes:UP000055136};
RN   [1] {ECO:0000313|EMBL:ALP54616.1, ECO:0000313|Proteomes:UP000055136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRL1 {ECO:0000313|EMBL:ALP54616.1};
RA   Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA   Strycharz-Glaven S.M.;
RT   "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT   Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL   Submitted (OCT-2015) 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; CP013099; ALP54616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2THK7; -.
DR   STRING; 1748243.Tel_16460; -.
DR   KEGG; tee:Tel_16460; -.
DR   Proteomes; UP000055136; 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: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; 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:UP000055136};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          8..37
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          59..82
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   408 AA;  44709 MW;  BF8168A5FFD37F9D CRC64;
     MPTLKITLAT QHQAERCVMC GLCLPHCPTY NKTQNEAESP RGRISLILGL AREQLQADDK
     LRSHLDNCLL CRACEVVCPS GVEFGTLMDG ARHALAQDRP RSEQRIPLDR LATDKQRQRR
     DAKLLWLADK TGLRALGRGL GLTRALGLAR FEQLAPEMRR PHDWQTYYPA RGETRGEVAL
     FIGCFSDMFD QATLDDSISL LTACGYGVHV PATQTCCGAL HQHSGDSASA RQLAQQNLDA
     FGALQLDAVI STATGCGAYL RDYEHIIGKA LPVCDINSFL SQIEWPDNLR MRPLNKRVAV
     HEPCSQRNVL KQADAPYVLL NRIPQLDLVS LPGNSQCCGA AGSYMIEHPA MADRLRQDKT
     DALARLSPDL LVSSNIGCAL HIAAGARAAG LRLEVVHPVT LLARQIAL
//
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