ID HISX_PSET1 Reviewed; 433 AA. AC Q3ICF0; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 106. 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=PSHAb0493; OS Pseudoalteromonas translucida (strain TAC 125). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z., RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica bacterium RT Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(2005). 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; CR954247; CAI89530.1; -; Genomic_DNA. DR AlphaFoldDB; Q3ICF0; -. DR SMR; Q3ICF0; -. DR STRING; 326442.PSHAb0493; -. DR KEGG; pha:PSHAb0493; -. DR PATRIC; fig|326442.8.peg.3401; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_0_6; -. DR BioCyc; PHAL326442:PSHA_RS17205-MONOMER; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000006843; Chromosome II. 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..433 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135818" FT ACT_SITE 325 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 326 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" 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 326 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 359 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 413 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 418 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 418 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 433 AA; 45811 MW; C517A5BA9A324F16 CRC64; MLRWNEESSQ AQAAALTRPA VSASAKVEAI CKTILAKVKE QGDDALLDMA KEFDNRANPR LRVPLDEINA SEQALSAELK YAIDTAYANV KCFHEAQLPK DIKLSTQPGV VCELKYQAIE AVGIYVPGGS APLPSSVIMQ GVLAQLSGAK TVVLATPVQG DKAINPAILY AAKLCGITTL IESGGAGAIA AMAYGTESVP KVNKIFGPGN SFVTMAKQLV AQTVPGMAID MPAGPSEVLV IADERANPEF IAADLLSQAE HGADSQVILL CNSESIIEQT QQALTRQLAK LSRKETAEQA LANSSLILVD SIAQAFDVSA QYGPEHLILQ LADSTPYLDK VKNAGSVFVG DYTPESAGDY ASGTNHVLPT YGYSASYSSL NLLDFFRTYT VQTITKSGLT QLSKAILPLA NAEGLDAHAN AVSIRLEAIK NEQ //