ID HISX_BACSU Reviewed; 427 AA. AC O34651; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 03-AUG-2022, entry version 135. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=BSU34910; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.; RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus RT subtilis."; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). 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 -!- 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; AF017113; AAC67295.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15496.1; -; Genomic_DNA. DR PIR; A69641; A69641. DR RefSeq; NP_391371.1; NC_000964.3. DR RefSeq; WP_003243286.1; NZ_JNCM01000033.1. DR AlphaFoldDB; O34651; -. DR SMR; O34651; -. DR STRING; 224308.BSU34910; -. DR PaxDb; O34651; -. DR EnsemblBacteria; CAB15496; CAB15496; BSU_34910. DR GeneID; 936584; -. DR KEGG; bsu:BSU34910; -. DR PATRIC; fig|224308.179.peg.3779; -. DR eggNOG; COG0141; Bacteria. DR InParanoid; O34651; -. DR OMA; MVTGPGN; -. DR PhylomeDB; O34651; -. DR BioCyc; BSUB:BSU34910-MON; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001570; 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 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 PANTHER; PTHR21256; PTHR21256; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 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..427 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135728" FT ACT_SITE 321 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 322 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 123 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 185 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 208 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 355 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 409 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 414 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 427 AA; 46256 MW; BDB0B2AE3C580E7F CRC64; MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK FDCIEIDSPL VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW FYHRKDGTML GQKVTALDSA GVYVPGGTAA YPSSVLMNVI PALVAGVERI VLVTPPGKDG LLSPGVLVAA AELGIKDIYK MGGAQAIAAL AYGTETIEPV DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET AIPSEIAADL LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE SIAAFARLEG LEAHARSIEA RERRISK //