ID G7WRF6_METH6 Unreviewed; 577 AA. AC G7WRF6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAR-2024, entry version 51. DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818}; DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818}; GN OrderedLocusNames=Mhar_2265 {ECO:0000313|EMBL:AET65617.1}; OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanotrichales; Methanotrichaceae; Methanothrix. OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65617.1, ECO:0000313|Proteomes:UP000005877}; RN [1] {ECO:0000313|EMBL:AET65617.1, ECO:0000313|Proteomes:UP000005877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6Ac {ECO:0000313|EMBL:AET65617.1, RC ECO:0000313|Proteomes:UP000005877}; RX PubMed=22590603; DOI=10.1371/journal.pone.0036756; RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.; RT "The genome characteristics and predicted function of methyl-group RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta RT spp."; RL PLoS ONE 7:E36756-E36756(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=[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; CP003117; AET65617.1; -; Genomic_DNA. DR RefSeq; WP_014587793.1; NC_017527.1. DR AlphaFoldDB; G7WRF6; -. DR STRING; 1110509.Mhar_2265; -. DR GeneID; 12511443; -. DR KEGG; mhi:Mhar_2265; -. DR PATRIC; fig|1110509.7.peg.2506; -. DR HOGENOM; CLU_020364_1_0_2; -. DR OrthoDB; 30771at2157; -. DR Proteomes; UP000005877; 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:SF8; 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:UP000005877}. FT DOMAIN 1..203 FT /note="Aldehyde ferredoxin oxidoreductase N-terminal" FT /evidence="ECO:0000259|SMART:SM00790" SQ SEQUENCE 577 AA; 63772 MW; 25038D771C76ACBD CRC64; MLRRVLYIDL GRGESAVEER EDLFEEWLGG TGVATQLLLE ECPPGADPLS PEAPIVFSIG PLNALFPAIT KTVAAFKSPL SGELGESYAG GRLGMALRFA GHEAVVVRGA AERPVYISIE NDEVKIKDAT SIWGVPATVV GYILRDVETG VGRRSIIRIG PGGERLVRYA GVVVDTYRHF GRLGLGAVFG SKKLKAIVVS GTEDVMVPDP RRYRRIYNRL FKTVVQTDAM EKYHDIGTPI NINVLNQLKG LPTRNFQDSS FEGAEKISGE VLADNYLFRR VSCAHCPIGC IHIGMLKTSF SREHEFEIRK ISYDFELLYA LGSNLGVSSA EGVLELIEAC ERQGLDAIST GVVLAWATEA LDRGLVTLQE TLGVSLRWND VPSYLKAIEN IVRMENEFYA ALAQGVVFAS ERYGGGEFAM ALGKNEVPGY HTGPASVVGL TVGVRHSHLD NAGYSIDQRA LKKSLTPEEM VDAIIREDDS RGVYNSLVGC LFARGVYTPE NILEALGSVG IEKTEGELEE LGRRIFDEKY RFKRREGFDL AEARIPRRFY ETVSAVGMID PETIEEMMRI YRKRRGW //