ID HISX_PSYA2 Reviewed; 431 AA. AC Q4FQF8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 123. 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=Psyc_1902; OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=259536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / VKM B-2377 / 273-4; RX PubMed=20154119; DOI=10.1128/aem.02101-09; RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., RA Murray A., Thomashow M., Tiedje J.M.; RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low- RT temperature growth."; RL Appl. Environ. Microbiol. 76:2304-2312(2010). 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; CP000082; AAZ19750.1; -; Genomic_DNA. DR RefSeq; WP_011281159.1; NC_007204.1. DR AlphaFoldDB; Q4FQF8; -. DR SMR; Q4FQF8; -. DR STRING; 259536.Psyc_1902; -. DR KEGG; par:Psyc_1902; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_6; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000546; Chromosome. 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; Histidine biosynthesis; Metal-binding; NAD; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..431 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135825" FT ACT_SITE 329 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 330 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 130 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 214 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 261 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 264 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 330 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 363 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 363 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 417 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 422 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 422 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 431 AA; 46506 MW; 0F4BC4043056A41D CRC64; MRQLSTQDAD FDSQLTELLA FETVNDATLL TTVDDIIARV RHGGDSVVLE LTQQFDQHPA TTTQALELSK EALAEAFANL DDVVKSALIT AATRVKTFHE RQVQETWQYE DELGNRLGQK VTALDRVGIY VPGGLASYPS SVLMNAIPAK VAGVKEVIMV VPAPKGVLNP LVLAAAHLAK VDRVFTIGGA QAVAALAYGT ETIPAVDKIT GPGNKYVAAA KRAVFGQVGI DMIAGPSEVL VYAEGEAQDR ADWLAMDLLS QAEHDRIAQA IFVTTSAQQL KEVAIEIEKA LAELPKADIA RDSLKNRGVL ILVRDREEGM AVINRVAPEH LELSVDHPDA LLNSIRHAGA IFMGRHTPEA IGDYCAGPNH VLPTSGTARF SSPLGVYDFQ KKSSIIYCSE SGSKPLAQTA DILAQHEDLE AHARSARYRY Q //