UniProt/TrEMBL: A0A160VTE7

Database: UniProt/TrEMBL
Entry: A0A160VTE7_9EURY

LinkDB:  A0A160VTE7_9EURY 
Original site:  A0A160VTE7_9EURY

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
All databases (19)   

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ID   A0A160VTE7_9EURY        Unreviewed;       607 AA.
AC   A0A160VTE7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   ORFNames=A3L04_08850 {ECO:0000313|EMBL:ASJ17168.1}, CHITON_0997
GN   {ECO:0000313|EMBL:CUX77776.1};
OS   Thermococcus chitonophagus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=54262 {ECO:0000313|EMBL:CUX77776.1, ECO:0000313|Proteomes:UP000093069};
RN   [1] {ECO:0000313|EMBL:CUX77776.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1 {ECO:0000313|EMBL:CUX77776.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000093069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Vorgias C.E.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ASJ17168.1, ECO:0000313|Proteomes:UP000250189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GC74 {ECO:0000313|EMBL:ASJ17168.1,
RC   ECO:0000313|Proteomes:UP000250189};
RA   Oger P.M.;
RT   "Complete genome sequence of Thermococcus chitonophagus type strain GC74.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC         carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001714};
CC   -!- COFACTOR:
CC       Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC         Evidence={ECO:0000256|ARBA:ARBA00001930};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the AOR/FOR family.
CC       {ECO:0000256|ARBA:ARBA00011032}.
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DR   EMBL; CP015193; ASJ17168.1; -; Genomic_DNA.
DR   EMBL; LN999010; CUX77776.1; -; Genomic_DNA.
DR   RefSeq; WP_068577332.1; NZ_LN999010.1.
DR   AlphaFoldDB; A0A160VTE7; -.
DR   STRING; 54262.CHITON_0997; -.
DR   GeneID; 33322685; -.
DR   KEGG; tch:CHITON_0997; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000093069; Chromosome i.
DR   Proteomes; UP000250189; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR   Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR   Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR   InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR   InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR   InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR   InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR   InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR   InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR   PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR30038:SF0; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   Pfam; PF01314; AFOR_C; 1.
DR   Pfam; PF02730; AFOR_N; 1.
DR   SMART; SM00790; AFOR_N; 1.
DR   SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR   SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CUX77776.1}; Tungsten {ECO:0000256|ARBA:ARBA00023245}.
FT   DOMAIN          4..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   607 AA;  67448 MW;  0C9C134F606A32B2 CRC64;
     MYGYWGKILR VNLSDGTIKE EKFDESFAKK WLGTRGFGIY YLLKEMDPKV DPFSPENKLI
     FATGPLTGTS APTGGRYMVI TKSPLTGYIA MANSGGYFGA ELKFAGWDAI IVEGKADHPV
     YIYINEDSVE IRDASHLWGK LVSETEEKLK EEVGDKNVQI ASIGPAGENK VRFAAVMNNG
     HRAAGRGGVG AVMGSKNLKA IVVRGRKRVE VADKGKFMEV VREKIEKLKK DPVAGGGLPK
     YGTAVLVNII NENGLYPTRN FQTGVFKYAY EQSGEAMAAK YLVRNKPCFA CPIGCGRVNK
     LPTLGETEGP EYESTWALGA NLGINDLAAI IEANHFADEY GMDTISLGGT LATAMELYER
     GLLKQEDIGG DNAPPFRFGN TEVLHYWIHK IATREGFGDI LAEGGYRLAE KFNGLEYFMG
     VKKQELPAYD PRGAEGHGLG YATNNRGGCH IKQYMISPEI LGYPYKMDPH DISDEKVKMV
     ILFQDLTALI DAAGLCVFTT FGLGADDYRD LLNAALGWDF STEDYLKIGE RIWNAERLFN
     LKAGLDPLKE DTLPKRLLEE PMPEGPHKGH VVRLKEMLPR YYKFRGWTED GRIPEEKLKE
     LELEEFM
//

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