ID HISX_BUCAP Reviewed; 435 AA. AC Q9ZHE6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=BUsg_093; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9767718; DOI=10.1007/s002849900392; RA Clark M.A., Baumann L., Baumann P.; RT "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes RT of histidine biosynthesis."; RL Curr. Microbiol. 37:356-358(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000250}. 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; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000305}. 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; AF067228; AAC97355.1; -; Genomic_DNA. DR EMBL; AE013218; AAM67663.1; -; Genomic_DNA. DR RefSeq; WP_011053629.1; NC_004061.1. DR AlphaFoldDB; Q9ZHE6; -. DR SMR; Q9ZHE6; -. DR STRING; 198804.BUsg_093; -. DR GeneID; 75259031; -. DR KEGG; bas:BUsg_093; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_0_6; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000416; 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; Zinc. FT CHAIN 1..435 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135746" FT ACT_SITE 327 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 328 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 189 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 328 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 361 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 415 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 435 AA; 47738 MW; CD25387C2B62BDE2 CRC64; MKYFNTIVNW NMLNSNEQKN ILLRPVIKNN NSIKKKVKKI IENIQVLGEK ALREYTILFE KCHINKFEVS KEKMLSSSLY VNQSLKDAIS TAKKNITSFH TAQILSPIDI ETQVGVRCQQ IYLPLNSVGI YIPSGIAPLF STVLMLAIPA KIAGCKQIIL CSPPPIDNTI LYAANICGVD KIFQMGGAQA IAALAFGTKN IPKVDKIFGP GNAYVTEAKL QVSSIFNGPQ IDMLAGPSEL LIIADEASNA DFIAADLLSQ AEHSISSQVI LLTPSLQLAK KVIISINNQL KNLSKSDDIS TALDNSVIIL TKDLFECIKI SNIYAPEHLI IQTKEPRLIL KEILNASSIF LGPWSPESAG DYASGTNHVL PTYGKSVSSS ALGLCDFKKR VLIQELTSQG FINLSNTLKI LSEAEKLEAH KNAVKIRVDF LKEKI //