ID M9YBC3_AZOVI Unreviewed; 436 AA. AC M9YBC3; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 29-MAY-2024, entry version 55. DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024, GN ECO:0000313|EMBL:AGK18080.1}; GN ORFNames=AvCA6_12930 {ECO:0000313|EMBL:AGK18080.1}; OS Azotobacter vinelandii CA6. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK18080.1, ECO:0000313|Proteomes:UP000012988}; RN [1] {ECO:0000313|EMBL:AGK18080.1, ECO:0000313|Proteomes:UP000012988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CA6 {ECO:0000313|EMBL:AGK18080.1, RC ECO:0000313|Proteomes:UP000012988}; RX PubMed=23792740; DOI=10.1128/genomeA.00313-13; RA Noar J.D., Bruno-Barcena J.M.; RT "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA RT 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. CC {ECO:0000256|HAMAP-Rule:MF_01024}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, CC ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01024}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRSR:PIRSR000099-4}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRSR:PIRSR000099-4}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000256|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}. 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; WP_012699939.1; NC_021150.1. DR AlphaFoldDB; M9YBC3; -. DR KEGG; avd:AvCA6_12930; -. DR PATRIC; fig|1283331.3.peg.1230; -. DR HOGENOM; CLU_006732_3_3_6; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000012988; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06572; Histidinol_dh; 1. DR Gene3D; 1.20.5.1300; -; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2. 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 NCBIfam; TIGR00069; hisD; 1. DR PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01024}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01024}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}. FT ACT_SITE 333 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT ACT_SITE 334 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT BINDING 136 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 220 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 268 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 334 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 367 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 367 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 421 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 426 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 426 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" 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 //