ID HISX_LEPBP Reviewed; 430 AA. AC B0SS41; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 90. 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=LEPBI_I1825; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=456481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides insights RT into the evolution of Leptospira and the pathogenesis of leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). 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; CP000786; ABZ97931.1; -; Genomic_DNA. DR RefSeq; WP_012388809.1; NC_010602.1. DR AlphaFoldDB; B0SS41; -. DR SMR; B0SS41; -. DR STRING; 456481.LEPBI_I1825; -. DR KEGG; lbi:LEPBI_I1825; -. DR HOGENOM; CLU_006732_3_0_12; -. DR OrthoDB; 9805269at2; -. DR BioCyc; LBIF456481:LEPBI_RS09020-MONOMER; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001847; Chromosome I. 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..430 FT /note="Histidinol dehydrogenase" FT /id="PRO_1000135439" FT ACT_SITE 324 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 325 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 185 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 208 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 233 FT /ligand="substrate" 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 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 325 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 358 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 412 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 430 AA; 47347 MW; 3D0CA083966873FA CRC64; MPIPILHCDR NSKELYSRFL QGAREDLTTA TDRILPILES VRTQGDQALF SYTEMFDGIK LSQLTIDPKK IKTNVDEKTK EAFLRAKSNI EAFHMEQKRE SWSKVIDGNR LGVKYTPIPS LAVYAPGGKA LYPSSVLMGI IPAKIAGVPS IQLITPPQKD GIPEILVWLA QIMDIDRIVT VGGAQGIAAA AYGTESVPKS EFIVGPGNAY VAAAKSYLSG QGLIGIESPA GPSEVCIIAD ENANPKWIAC DMLSQAEHGE DSSAILLTTD LTLAKRVSEE LEIAFSERPK RLQMKQTAIY ENSSILVFPT LDDCIWFSNE LAPEHLEIQT KDYESVFAKI EHAGSVFLGP YSPVAMGDYI SGTNHILPTA RGSRIYSSLG VDTFLKRVTF QEVTKESLEN LYPFVKLMSE LEGLDEEHGT SVKVRTRQFQ //