ID I6V105_9EURY Unreviewed; 622 AA. AC I6V105; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 24-JAN-2024, entry version 49. DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818}; DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818}; GN ORFNames=PFC_08775 {ECO:0000313|EMBL:AFN04680.1}; OS Pyrococcus furiosus COM1. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=1185654 {ECO:0000313|Proteomes:UP000006216}; RN [1] {ECO:0000313|EMBL:AFN04680.1, ECO:0000313|Proteomes:UP000006216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COM1 {ECO:0000313|EMBL:AFN04680.1, RC ECO:0000313|Proteomes:UP000006216}; RX PubMed=22636780; DOI=10.1128/JB.00439-12; RA Bridger S.L., Lancaster W.A., Poole F.L.II., Schut G.J., Adams M.W.; RT "Genome Sequencing of a Genetically-Tractable Pyrococcus furiosus Strain RT Reveals a Highly Dynamic Genome."; RL J. Bacteriol. 194:4097-4106(2012). 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; CP003685; AFN04680.1; -; Genomic_DNA. DR RefSeq; WP_011013103.1; NC_018092.1. DR AlphaFoldDB; I6V105; -. DR GeneID; 41713783; -. DR KEGG; pfi:PFC_08775; -. DR PATRIC; fig|1185654.4.peg.1784; -. DR HOGENOM; CLU_020364_1_0_2; -. DR Proteomes; UP000006216; 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..203 FT /note="Aldehyde ferredoxin oxidoreductase N-terminal" FT /evidence="ECO:0000259|SMART:SM00790" SQ SEQUENCE 622 AA; 69369 MW; C949C9E10DFF5CFC CRC64; MFGYKGKIAR VNLTTGKVKY EDLPEEIIRK FIGGKGLGYY IIYKEVPPGT DPLSPANKFV FATGGLTGLV PGGSKVIAVS KSPTTRLITD SSGGDAFGPK LKGHFDALII EGRSEEPVYL YIHDGKVEIN PAEHLWGKGT YEVAKEIWKD HPSASIAMIG PAGEKMSRMA NVVYDTERAS GRGGLGAVLG SKRVKAIVVE PGERPKVAHT EEFQQLWSEF YKKFSTDPKY ADTRKYGTTT ALLWAAEVGM GSAYNFSKPH IPEELAKKLS GLEIERYEIE PEWYIHGKSC PIKCSMYMEI EYKGKKIRVK PEYESLGMLG AATGVFDLPA VSYFIWLVNN YGLDSIATGN TIAWFLELVE RGLITEEEIG FPVKGFGDAE AVERLIHLIA ERKGIGAVLA DGVKRACERL GRGCEFAVHV KGLESPAWDP RGRRTYALSY ATADIGASHL RGWPSPHQLP NDGPAKELVP SLIEDRDYMY IINMLGVCKF VPYTLDDLAK LYSLATGEEW SVEKLRRVAQ AVESMARIYN ALEWITPPLD DTIPPRWWEP EKDGPAKGNA AFIDYNDFLE ARREFYRLRG WDEELGVPLP ETMEKLGYPE FKEDAKRALE VVKRRMLNTA LS //