ID   HISX_CORDI              Reviewed;         449 AA.
AC   P60858;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-NOV-2008, entry version 37.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=DIP1566;
OS   Corynebacterium diphtheriae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   MEDLINE=22965443; PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L.,
RA   Whitehead S., Barrell B.G., Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium
RT   diphtheriae NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248358; CAE50091.1; -; Genomic_DNA.
DR   RefSeq; NP_939908.1; -.
DR   GeneID; 2650755; -.
DR   GenomeReviews; BX248353_GR; DIP1566.
DR   KEGG; cdi:DIP1566; -.
DR   NMPDR; fig|257309.1.peg.1499; -.
DR   HOGENOM; P60858; -.
DR   BioCyc; CDIP257309:DIP1566-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    449       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135759.
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   ACT_SITE    344    344       Proton acceptor (By similarity).
FT   METAL       274    274       Zinc (By similarity).
FT   METAL       277    277       Zinc (By similarity).
FT   METAL       377    377       Zinc (By similarity).
FT   METAL       436    436       Zinc (By similarity).
FT   BINDING     135    135       NAD (By similarity).
FT   BINDING     199    199       NAD (By similarity).
FT   BINDING     229    229       NAD (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
FT   BINDING     274    274       Substrate (By similarity).
FT   BINDING     277    277       Substrate (By similarity).
FT   BINDING     344    344       Substrate (By similarity).
FT   BINDING     377    377       Substrate (By similarity).
FT   BINDING     431    431       Substrate (By similarity).
FT   BINDING     436    436       Substrate (By similarity).
SQ   SEQUENCE   449 AA;  47762 MW;  002BB36B98F433FB CRC64;
     MRKRKIMLNV IDLRGHVPTT SELRRTLPRG GTDINSVLPI VEPVVTDVKN RGAAAALDYG
     EKFDHVRPTS IRVPQDVIDQ ALDSLDPNVI EALKESIARV RAVHSEQLPA QHTTSFGEGA
     TITEKFIPVS RVGLYAPGGN AVYPSSVIMN VVPAQEAGVE SLVVASPPQK DHGGWPHPTI
     LAAAKLLGVT EVWAMGGAQA VALLAYGDDT QQNSAEVLEP VDMITGPGNI FVTAAKRLVR
     GVVGIDSEAG PTEIAIVADA QANPVWIAYD LISQAEHDVL AASVLITDSE ELAQRVNEEV
     AARYSVTRNA DRVSEALKGQ QSGIVLVDDL PTAVIVADAY AAEHLEIHTA ESHKVAEQIR
     NAGAIFVGGY SPVPLGDYSA GSNHVLPTSG SARYSSGLST HTFLKPVNVI YYDEVALKEI
     SDTVITLADA EDLPAHGEAI RTRFENLGN
//