ID HISX_HALSA Reviewed; 425 AA. AC Q9HPW5; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; GN OrderedLocusNames=VNG_1444G; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001. OX NCBI_TaxID=64091; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R., RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., RA DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01024}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01024}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01024}. 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; AE004437; AAG19752.1; -; Genomic_DNA. DR PIR; D84298; D84298. DR RefSeq; WP_010903049.1; NC_002607.1. DR AlphaFoldDB; Q9HPW5; -. DR SMR; Q9HPW5; -. DR STRING; 64091.VNG_1444G; -. DR PaxDb; 64091-VNG_1444G; -. DR GeneID; 68694160; -. DR KEGG; hal:VNG_1444G; -. DR PATRIC; fig|64091.14.peg.1102; -. DR HOGENOM; CLU_006732_3_0_2; -. DR InParanoid; Q9HPW5; -. DR OrthoDB; 36308at2157; -. DR PhylomeDB; Q9HPW5; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central. 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; IBA:GO_Central. 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; Histidine biosynthesis; Metal-binding; NAD; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..425 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135892" FT ACT_SITE 321 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 322 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 124 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 184 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 207 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 355 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 409 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 414 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 425 AA; 44457 MW; BC8C770AE42A007B CRC64; MEYEAVADLA PDRRVALFER DAGVDAVRSD VAEILDRVES EGDVALRALA SEFDDVEVGN LDVTDEMERA ADAVPDDVYD AIEDAAANIR AFHEAQLPDD WRESFAAGRE LGRRFRPVRR VGVYAPGGTA AYPSSVLMGV IPAVVAGVEQ VAVATPPAET INPVTLAAAH AAGADRVYQV GGAQAIGAFA YGTETVDTVQ TVVGPGNKWV TAAKAEVRGD VEIDFLAGPS ELLVVADETA EPAFVAADLL AQAEHDPNAS VVAVTDDEAT AAAITDAVAA RLDDRERADT IRAALDNEAS GVFVARSMSE AVMFAEEYAA EHLSIQASDD EALLDRIDSA GSVFLGGYAP VAAGDYAAGT NHVLPTNGTA RVTGGLSVDT FLRSTTVQRL DREGLAALRE TVTTLADAEG LEGHAASVDA RFEDE //