ID D8K627_NITWC Unreviewed; 456 AA. AC D8K627; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; GN OrderedLocusNames=Nwat_1444 {ECO:0000313|EMBL:ADJ28354.1}; OS Nitrosococcus watsoni (strain C-113). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Nitrosococcus. OX NCBI_TaxID=105559 {ECO:0000313|EMBL:ADJ28354.1, ECO:0000313|Proteomes:UP000000393}; RN [1] {ECO:0000313|EMBL:ADJ28354.1, ECO:0000313|Proteomes:UP000000393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-113 {ECO:0000313|EMBL:ADJ28354.1, RC ECO:0000313|Proteomes:UP000000393}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Malfatti S.A., Chain P.S.G., Land M., Hauser L., Kyrpides N., RA Ivanova N., Cambell M.A., Heidelberg J.F., Klotz M.G., Woyke T.; RT "Complete sequence of chromosome of Nitrosococcus watsoni C-113."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492, CC ECO:0000256|RuleBase:RU003345}. 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; CP002086; ADJ28354.1; -; Genomic_DNA. DR AlphaFoldDB; D8K627; -. DR STRING; 105559.Nwat_1444; -. DR KEGG; nwa:Nwat_1444; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_3_1_6; -. DR OrthoDB; 9812625at2; -. DR Proteomes; UP000000393; Chromosome. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR036492}. FT DOMAIN 20..427 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 209 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 243 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1" SQ SEQUENCE 456 AA; 52079 MW; 86A1FBE96550EE17 CRC64; MTDFRPLMRA FFSAGNTRNY AFRRQQLQSL HRLIFEHEEE IIRVLAADFG KPTAETYASE IAFLYQEINH TLKHLRNWMR PKKVSTPLVL QPSKSRIYFE PKGVVLVVGP WNYPFQLTLA PVVAAMAAGN CVVIKPSELT PQTSALIKHL INNYFSPEYL VVVEGEGAQI VPELIDKYHF DHIFFTGSTR VGAMIAEQAG RHLISTTLEL GGKSPAIVER SATFEVAARR LLWGKFFNSG QTCVAPDYLL LDEEIADSFI EILKNNLLKF YDDPSQASRH LARIVGKERW KTLVGYLEQG KILYGGQYNE ERLYIAPTLL QVTDLSQSVM QEEIFGPILP IITYQNCSEA LEIIERNPYP LAFYLFTREK KKQNWYLEHV QFGGGAINNA MVHLSNPNLP FGGINQSGHG RYHGYEGFSA FSNHKSVLHS DTWFDPDFKY PPYSKTTLKW FRRLLG //