ID Q3A1K5_SYNC1 Unreviewed; 628 AA. AC Q3A1K5; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 90. DE SubName: Full=Aldehyde:ferredoxin oxidoreductase, tungsten-containing {ECO:0000313|EMBL:ABA89752.1}; GN OrderedLocusNames=Pcar_2514 {ECO:0000313|EMBL:ABA89752.1}; OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) OS (Pelobacter carbinolicus). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales; OC Syntrophotaleaceae; Syntrophotalea. OX NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA89752.1, ECO:0000313|Proteomes:UP000002534}; RN [1] {ECO:0000313|Proteomes:UP000002534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1 RC {ECO:0000313|Proteomes:UP000002534}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelobacter carbinolicus DSM 2380."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABA89752.1, ECO:0000313|Proteomes:UP000002534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1 RC {ECO:0000313|Proteomes:UP000002534}; RX PubMed=23227809; DOI=10.1186/1471-2164-13-690; RA Aklujkar M., Haveman S.A., Didonato R.Jr., Chertkov O., Han C.S., RA Land M.L., Brown P., Lovley D.R.; RT "The genome of Pelobacter carbinolicus reveals surprising metabolic RT capabilities and physiological features."; RL BMC Genomics 13:690-690(2012). 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; CP000142; ABA89752.1; -; Genomic_DNA. DR RefSeq; WP_011342288.1; NC_007498.2. DR AlphaFoldDB; Q3A1K5; -. DR STRING; 338963.Pcar_2514; -. DR KEGG; pca:Pcar_2514; -. DR eggNOG; COG2414; Bacteria. DR HOGENOM; CLU_020364_1_0_7; -. DR OrthoDB; 9763894at2; -. DR Proteomes; UP000002534; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro. 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:UP000002534}. FT DOMAIN 5..209 FT /note="Aldehyde ferredoxin oxidoreductase N-terminal" FT /evidence="ECO:0000259|SMART:SM00790" SQ SEQUENCE 628 AA; 68614 MW; D98A78729A2C4C03 CRC64; MLGGYWQKIA VIDLTNETVE YIEPSEDDLK KYIGGSGLGA KLLYENTAPG IDPLGPENVL ICMTGPYVGT KVAQSGRWEL ITKGPLTGIY LESDCGGKWG ATLKSCGLDG LMVKGKAKQP VYVTIVDDDI QIKKADKLWG KGTFDTDKIL KEELGRGSQA ISIGQAGEKL VKFAAIMTDG REGRAAGRGG GGAVMGSKNL KAIACKGSKK VAIARPEPYE ELVKEIRAKT KEVYDGPLGT YGTSCAVEIF NDCGDLPIKN WLWGTWDKAA KVSGQELAKT VLKKRYHCGG CLIGCGRTVE IPAGAFKMKE GGGPEYETLG LLGSNCLVDD VEAICKGNEI CNDYGVDTIE AAGIISFLME AWEHGMIDEG DTDGLEMTWG NGLAMCEMLE KVCLRKGIGD PCSQGIFEAV KRVGPASEEF AIHTKGMMFP AHDPRGRGGL GVAYATSNRG ACHMQAYNQD FEGEGCFNIA DLGYDAPLPP YTNEGKGKFV ADQQHFMSMM DSLKLCKFSI FGGMTVGPMT QFLNHIVGWD FTNEQWLECG ERIFNLKRLF NTREGVSRKD DTLPPRILAS PRQGGSGDYV PDLGYMLRDY YRARGWDEWG IPTPETLKRL SLDKYEYRKG ERTTENQR //