ID HISX_NEIMB Reviewed; 429 AA. AC Q9JYH8; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 122. 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=NMB1581; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(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; AE002098; AAF41934.1; -; Genomic_DNA. DR PIR; E81067; E81067. DR RefSeq; NP_274587.1; NC_003112.2. DR RefSeq; WP_002220532.1; NC_003112.2. DR AlphaFoldDB; Q9JYH8; -. DR SMR; Q9JYH8; -. DR STRING; 122586.NMB1581; -. DR PaxDb; 122586-NMB1581; -. DR GeneID; 61281748; -. DR KEGG; nme:NMB1581; -. DR PATRIC; fig|122586.8.peg.2032; -. DR HOGENOM; CLU_006732_3_3_4; -. DR InParanoid; Q9JYH8; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; 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..429 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135802" FT ACT_SITE 327 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 328 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 259 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 262 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 328 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 361 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 415 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 429 AA; 46324 MW; 1A6597DF1E685847 CRC64; MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE YTNKFDQTNA KSIDDLILTQ ADLNAAFERI PNDVQTALQT AARRVESYHQ RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAVAALAYGT ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA SLGNRGAMIL AKDLDEACEI ANYISPEHLE LSVENPQEWA KKIRHAGAIF MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG AQKLGETASV LAHGESLTAH ARAAEFRMK //