ID A2BLI7_HYPBU Unreviewed; 621 AA. AC A2BLI7; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818}; DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818}; GN OrderedLocusNames=Hbut_1001 {ECO:0000313|EMBL:ABM80848.1}; OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae; OC Hyperthermus. OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80848.1, ECO:0000313|Proteomes:UP000002593}; RN [1] {ECO:0000313|EMBL:ABM80848.1, ECO:0000313|Proteomes:UP000002593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5 RC {ECO:0000313|Proteomes:UP000002593}; RX PubMed=17350933; RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., RA She Q., Garrett R.A., Klenk H.P.; RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."; RL Archaea 2:127-135(2007). 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=[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; CP000493; ABM80848.1; -; Genomic_DNA. DR RefSeq; WP_011822166.1; NC_008818.1. DR AlphaFoldDB; A2BLI7; -. DR STRING; 415426.Hbut_1001; -. DR EnsemblBacteria; ABM80848; ABM80848; Hbut_1001. DR GeneID; 4782804; -. DR KEGG; hbu:Hbut_1001; -. DR eggNOG; arCOG00706; Archaea. DR HOGENOM; CLU_020364_1_0_2; -. DR OrthoDB; 30771at2157; -. DR Proteomes; UP000002593; 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:ABM80848.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002593}. FT DOMAIN 1..207 FT /note="Aldehyde ferredoxin oxidoreductase N-terminal" FT /evidence="ECO:0000259|SMART:SM00790" SQ SEQUENCE 621 AA; 69288 MW; 10603EB8E397E337 CRC64; MEFKLLRINL WTQKVREEKI DERTLRRFLG GRGLGAYLAL KEIPKGADPL GPENKLYILT GPLTGTAAVE TGRYHVVGKS PLTGILGDSN SGGQFGPWLR FSGYDGIVLE SVSEEPVWIS IIDGEVKFHD ARDLWGRGVI YTEKKIRDRV GITKPDLGSV LSIGPAGENL SKIAAIMNDK YRAAGRTGLG AVMGSKRVKA IFVYGHRRIE LYDRQKFLEA AKKLSKAIVE HSISQSLTKY GTAVLVNIIN EHGGLPTKNW TRGVFEKAQQ ISGEYLAEHY LKTNKGCWGC AIRCSRVAEV KSGPYRTPVS EGPEYETIWA NGANTMIGNM EAIIKINYLL NDMGLDTISF GNTAATLMEL YEKAQKGELP EDKAKKLLDL LEDVEPTWGN ADAVIRLIWK TAYRDGIGDY TAEGAARLAE EFGCPDCAIH VRGLELPAYD PRAINSMALS YATSNRGGCH LRAYGVSFDV LGVPKKFDPL KIDLEKVKLI KWQQDYFAVI DSLVVCKFNT FADAPEYYVE LLKYAMGWED LTVEELLTIG ERIYNVERLF AVREGRGYRD YLPKRLLEEP LPDGPAKGRT AKEALETYLP EYYKLRGWVD GKPTPETLKR LGLGEFLYIV A //