ID   HISX_BACCR              Reviewed;         429 AA.
AC   Q81G06;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 40.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=BC_1406;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08387.1; -; Genomic_DNA.
DR   RefSeq; NP_831186.1; -.
DR   GeneID; 1203755; -.
DR   GenomeReviews; AE016877_GR; BC_1406.
DR   KEGG; bce:BC1406; -.
DR   HOGENOM; Q81G06; -.
DR   BioCyc; BCER226900:BC_1406-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_0000135722.
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;  47511 MW;  421984C965563315 CRC64;
     MEIIYEEFKE ALSKIKVLRE NANIIEETVQ RSVREIIRHV REGKDEALSF YTKKFDGVEM
     KNFRVSEEEI QQASMFVENS FLEALKEAKK NVVSYHEKQK KHSIFDCESK GIIRGQLIRP
     LENIGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP RKGGIDPHIL AAADLAGVDE
     IYTIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVVA
     DETGNAKYIA ADLLSQAEHD ERATAICITT NMELAKEVEK EVERQLETLP RSEIARESIN
     RNGAIFIVPS LEEALKLSNE IAPEHLELHI KEPMNALDYV KHAGSIFLGP YSPEPLGDYL
     AGPNHVLPTS GTARFFSPLS VDDFVKKSSF ISYTEEALKN VQHHIVELAN KEGLHAHARA
     IQIRFEEEK
//