ID Q0K687_CUPNH Unreviewed; 446 AA. AC Q0K687; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 118. 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:CAJ94484.1}; GN OrderedLocusNames=H16_A3416 {ECO:0000313|EMBL:CAJ94484.1}; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ94484.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ94484.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337 {ECO:0000313|Proteomes:UP000008210}; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01024, 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; AM260479; CAJ94484.1; -; Genomic_DNA. DR RefSeq; WP_010812332.1; NZ_CP039287.1. DR AlphaFoldDB; Q0K687; -. DR STRING; 381666.H16_A3416; -. DR GeneID; 57645546; -. DR KEGG; reh:H16_A3416; -. DR PATRIC; fig|381666.6.peg.3809; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_4; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000008210; Chromosome 1. 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}; Reference proteome {ECO:0000313|Proteomes:UP000008210}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}. FT ACT_SITE 341 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT ACT_SITE 342 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT BINDING 144 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 205 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 228 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 251 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 273 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 273 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 276 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 276 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 342 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 375 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 375 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 429 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 434 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 434 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" SQ SEQUENCE 446 AA; 47806 MW; EF335B2EB27D7B0F CRC64; MNATEMENLP IRRLDSSKPG FAEALRQVLA FEAGEDEAID RAAAQILADV KARGDAAVLE YTRRFDRVEA SSMGALEVSQ QQLEAALEDL EPKRRAALEA AAARVRAYHE KQKIECGSHS WEYTEADGTM LGQKVTPLDR VGIYVPGGKA AYPSSVLMNA IPARVAGVKE IIMVVPTPGG VRNELVLAAA QIAGVDRVFT IGGAQAIGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG TVGIDMIAGP SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAG YIARVEASIQ RQLGTMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP RQWSEKIRHA GAIFLGPYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD FQKRSSLIEV SEGGAQMLGQ IAAELAYGEG LQAHARSAEY RFTKRS //