GenomeNet

Database: UniProt/TrEMBL
Entry: W8NRN4_9EURY
LinkDB: W8NRN4_9EURY
Original site: W8NRN4_9EURY 
ID   W8NRN4_9EURY            Unreviewed;       619 AA.
AC   W8NRN4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   ORFNames=BD01_0256 {ECO:0000313|EMBL:AHL21883.1};
OS   Thermococcus nautili.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL21883.1, ECO:0000313|Proteomes:UP000019434};
RN   [1] {ECO:0000313|EMBL:AHL21883.1, ECO:0000313|Proteomes:UP000019434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30-1 {ECO:0000313|EMBL:AHL21883.1,
RC   ECO:0000313|Proteomes:UP000019434};
RA   Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA   Forterre P.;
RT   "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT   1, producing viral vesicles.";
RL   Submitted (FEB-2014) 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}.
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; CP007264; AHL21883.1; -; Genomic_DNA.
DR   RefSeq; WP_042689103.1; NZ_CP007264.1.
DR   AlphaFoldDB; W8NRN4; -.
DR   STRING; 195522.BD01_0256; -.
DR   GeneID; 24958185; -.
DR   KEGG; tnu:BD01_0256; -.
DR   eggNOG; arCOG00709; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000019434; 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   Tungsten {ECO:0000256|ARBA:ARBA00023245}.
FT   DOMAIN          4..204
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   619 AA;  69108 MW;  561DE9B30DD2864A CRC64;
     MYGYKNRIAR VNLTEGKVTY EELPDEVIRK FVGGKGLGYY LIYREVPPGT DPLSPANKFV
     FATGGLTGLI PGSSKVIAVS KSPETRLISD SSGGDAFGPK LKGHFDAIII EGKAEEPVYL
     YVHDGEVEIR DAKHLWGRGN YEVAKELWKE HPKASLALIG PAGERLSRIA NVIYDTERAS
     GRGGLGAVLG SKKVKAVVVE PGEKPPVASP EEFQRLWQEF YDHFATDPKY EHSRNYGTSD
     ALRSSASLGM SPAYNFSRPY IPEELAEKLG GDEVKKYEVE PEWFVHGKSC PIKCARYVEV
     EYKGRKIRVK PEYESIAMLG AATGVFNFPA VAYFNWLVNN LGLDSIATGA TIGWFFELVE
     RGLISEEEIG FPVRGFGDEE AEEKLIKLMA EKKGIGAILA DGVKRACERL GRGCEFAVHV
     KGMESPAWDP RGRRTYALSY ATADVGASHL RGWPRPHQLP NQGPAKELVP SLIEGRDESY
     ITDMLGTCKF VSYKMEDLAR FYSLATGEEW TVKRLRKIAQ AVESIARIHD ALDWVTPPLD
     DTIPPRWWEP EPDGPAKGNA AFIDYNDFLE ARKEFYRLRG WHEELGVPLP ETMEELGYPE
     FKSDAERALE VVRKRMGVE
//
DBGET integrated database retrieval system