ID Q5JI10_THEKO Unreviewed; 621 AA. AC Q5JI10; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818}; DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818}; GN OrderedLocusNames=TK0844 {ECO:0000313|EMBL:BAD85033.1}; OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OS (Pyrococcus kodakaraensis (strain KOD1)). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD85033.1, ECO:0000313|Proteomes:UP000000536}; RN [1] {ECO:0000313|EMBL:BAD85033.1, ECO:0000313|Proteomes:UP000000536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1 RC {ECO:0000313|Proteomes:UP000000536}; RX PubMed=15710748; DOI=10.1101/gr.3003105; RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus RT kodakaraensis KOD1 and comparison with Pyrococcus genomes."; RL Genome Res. 15:352-363(2005). 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; AP006878; BAD85033.1; -; Genomic_DNA. DR RefSeq; WP_011249795.1; NC_006624.1. DR AlphaFoldDB; Q5JI10; -. DR STRING; 69014.TK0844; -. DR EnsemblBacteria; BAD85033; BAD85033; TK0844. DR GeneID; 78447359; -. DR KEGG; tko:TK0844; -. DR PATRIC; fig|69014.16.peg.824; -. DR eggNOG; arCOG00709; Archaea. DR HOGENOM; CLU_020364_1_0_2; -. DR InParanoid; Q5JI10; -. DR OrthoDB; 30771at2157; -. DR PhylomeDB; Q5JI10; -. DR Proteomes; UP000000536; 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 Reference proteome {ECO:0000313|Proteomes:UP000000536}; 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 621 AA; 69177 MW; 21F24DDC52E04350 CRC64; MYGYQNKIAR VNLTTGKVTY EELPDEVIRK FIGGKGLGYY IIYREVPPGT DPLSPANKFV FAAGGLTGLV PGSSKVIAIS KSPETRLISD SSGGDAFGPK LRGHFDALII EGKSEEPVYL YIHDGKVEIK DASHLWGKGN YEVAKELWKE YPTASMAMVG PAGERLSRIA DIIYDTERAS GRGGLGAVLG SKRVKAVVVE PGEKPKVAEP EEFQRLWQEY YNEFATNPKY EHTRTYGTTD ALRSAASLGM SPAYNFSRPY IPDELASKLG GDEVKKYEVE PEWFVHGKSC PIKCARYVEV EYKGKKIRVK PEYESIAMLG AATGVFDFPA VAYFIHLVND YGMDSIATGA TIGWLFEMVE RGLISEDEIG FPVKGFGDAE AEERLIKLMA ERKGIGAILA DGVKRACERL GRGCEFAVHV KGMESPAWDP RGRRTYGLSY ATADVGASHL RGWPRPHQLP NQGPAKELVP SLIEGRDESY ITDMLGTCKF VPYKMEDLAK LYSVATGEEW TVEELRKRAW GVESIARIHD ALDWVTPPLD DTIPPRWWEP EPDGPAKGNA AFIDYNDFLE ARREFYRLRG WHEELGVPLP ETMEKLGLPE FKEDAARAID VVKKRMEFSG Q //