ID   HISX_BACCZ              Reviewed;         429 AA.
AC   Q63DX2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 32.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=BCE33L1291;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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.
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DR   EMBL; CP000001; AAU18958.1; -; Genomic_DNA.
DR   RefSeq; YP_082890.1; -.
DR   GeneID; 3023156; -.
DR   GenomeReviews; CP000001_GR; BCE33L1291.
DR   KEGG; bcz:BCZK1291; -.
DR   HOGENOM; Q63DX2; -.
DR   BioCyc; BCER288681:BCE33L1291-MON; -.
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    429       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135723.
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   ACT_SITE    325    325       Proton acceptor (By similarity).
FT   METAL       256    256       Zinc (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       358    358       Zinc (By similarity).
FT   METAL       417    417       Zinc (By similarity).
FT   BINDING     127    127       NAD (By similarity).
FT   BINDING     188    188       NAD (By similarity).
FT   BINDING     211    211       NAD (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     325    325       Substrate (By similarity).
FT   BINDING     358    358       Substrate (By similarity).
FT   BINDING     412    412       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
SQ   SEQUENCE   429 AA;  47271 MW;  EBF5F9843321CD2C CRC64;
     MEIVCEDFQK ALTKIKLLRE NANIIEETVQ RSVREIVQNV RESRDEALSF YTKKFDGVEI
     KDVRVSEEEI KQASMFVESS FLEALQEAKK NIISYHEKQK RQSMFDCTSK GIIRGQIIRP
     LENIGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP RAGGIDPHIL VAASLAGVDE
     IYMIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA
     DETGNAKYIA ADLLSQAEHD ERATAICITT NIELAKEVEK EIERQLETLP RSEIARESIN
     RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP YAPEPLGDYL
     AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD VKHHIVELAN KEGLHAHARS
     IQIRFGEEE
//