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 20-JAN-2009, entry version 64. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=BSU34910; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., RA 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 MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2 CC NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. 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; Z99121; CAB15496.1; -; Genomic_DNA. DR PIR; A69641; A69641. DR RefSeq; NP_391371.1; -. DR HSSP; P06988; 1K75. DR GeneID; 936584; -. DR GenomeReviews; AL009126_GR; BSU34910. DR KEGG; bsu:BSU34910; -. DR NMPDR; fig|224308.1.peg.3497; -. DR SubtiList; BG12599; hisD. DR HOGENOM; O34651; -. DR BioCyc; BSUB224308:BSU3488-MON; -. DR BRENDA; 1.1.1.23; 150. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01024; -; 1. DR InterPro; IPR001692; Histidinol_DHase. DR InterPro; IPR012131; Hstdl_DHase_prok. DR PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR ProDom; PD002680; Histidinol_dh; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1 427 Histidinol dehydrogenase. FT /FTId=PRO_0000135728. FT ACT_SITE 321 321 Proton acceptor (By similarity). FT ACT_SITE 322 322 Proton acceptor (By similarity). FT METAL 253 253 Zinc (By similarity). FT METAL 256 256 Zinc (By similarity). FT METAL 355 355 Zinc (By similarity). FT METAL 414 414 Zinc (By similarity). FT BINDING 123 123 NAD (By similarity). FT BINDING 185 185 NAD (By similarity). FT BINDING 208 208 NAD (By similarity). FT BINDING 231 231 Substrate (By similarity). FT BINDING 253 253 Substrate (By similarity). FT BINDING 256 256 Substrate (By similarity). FT BINDING 322 322 Substrate (By similarity). FT BINDING 355 355 Substrate (By similarity). FT BINDING 409 409 Substrate (By similarity). FT BINDING 414 414 Substrate (By similarity). 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 //