ID M9YBC3_AZOVI Unreviewed; 436 AA. AC M9YBC3; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 22-JAN-2014, entry version 6. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; ORFNames=AvCA6_12930; OS Azotobacter vinelandii CA6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=1283331; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CA6; RA Noar J.D., Bruno-Barcena J.M.; RT "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain RT CA and Tungsten-Tolerant Mutant Strain CA6."; RL Genome Announc. 1:E00313-E00313(2013). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine CC + 2 NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. 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; CP005095; AGK18080.1; -; Genomic_DNA. DR RefSeq; YP_007897353.1; NC_021150.1. DR ProteinModelPortal; M9YBC3; -. DR EnsemblBacteria; AGK18080; AGK18080; AvCA6_12930. DR GeneID; 15368198; -. DR KEGG; avd:AvCA6_12930; -. DR KO; K00013; -. DR UniPathway; UPA00031; UER00014. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01024; HisD; 1; -. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Zinc. FT ACT_SITE 333 333 Proton acceptor (By similarity). FT ACT_SITE 334 334 Proton acceptor (By similarity). FT METAL 265 265 Zinc (By similarity). FT METAL 268 268 Zinc (By similarity). FT METAL 367 367 Zinc (By similarity). FT METAL 426 426 Zinc (By similarity). FT BINDING 136 136 NAD (By similarity). FT BINDING 197 197 NAD (By similarity). FT BINDING 220 220 NAD (By similarity). FT BINDING 243 243 Substrate (By similarity). FT BINDING 265 265 Substrate (By similarity). FT BINDING 268 268 Substrate (By similarity). FT BINDING 334 334 Substrate (By similarity). FT BINDING 367 367 Substrate (By similarity). FT BINDING 421 421 Substrate (By similarity). FT BINDING 426 426 Substrate (By similarity). SQ SEQUENCE 436 AA; 47154 MW; 5670516359A6DD6E CRC64; MTTSLALRRL DAADPDFPRH LDYLLSWESV SDEAVNRRVL DILQAVRERG DAAVVEFTRR FDNVEAGSMA ELILPRERLE LALTRISPEQ REALEKAAGR VRLYHERQKQ DSWTYTEADG TVLGQQITPL DRAGLYVPGG KAAYPSSVLM NAIPAKVAGV AEVVMVVPTP RGELNELVLA AACVAGVDRV FTIGGAQAVA ALAYGTESVP QVDKIVGPGN IYVATAKRHV FGQVGIDMIA GPSEILVVCD GQSDPDWIAM DLFSQAEHDE DAQSILVSPD ADFLERVAES IARLLPTMER AEIIRTSLEG RGALIRVTDL EQAIAVANRI APEHLELSVA DPQRWLPKIR HAGAIFMGRY TAEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII FCSAAGASEL GETASVLARG ESLTAHARSA EYRIKA //