ID   HISX_COREF              Reviewed;         451 AA.
AC   Q8FNZ0;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=CE2003;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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; BA000035; BAC18813.1; -; Genomic_DNA.
DR   RefSeq; NP_738613.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1032060; -.
DR   GenomeReviews; BA000035_GR; CE2003.
DR   KEGG; cef:CE2003; -.
DR   NMPDR; fig|196164.1.peg.2003; -.
DR   HOGENOM; Q8FNZ0; -.
DR   OMA; Q8FNZ0; LGVETFM.
DR   BioCyc; CEFF196164:CE2003-MON; -.
DR   BRENDA; 1.1.1.23; 277326.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
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_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH_prok-type.
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    451       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135760.
FT   ACT_SITE    332    332       Proton acceptor (By similarity).
FT   ACT_SITE    333    333       Proton acceptor (By similarity).
FT   METAL       263    263       Zinc (By similarity).
FT   METAL       266    266       Zinc (By similarity).
FT   METAL       366    366       Zinc (By similarity).
FT   METAL       425    425       Zinc (By similarity).
FT   BINDING     129    129       NAD (By similarity).
FT   BINDING     193    193       NAD (By similarity).
FT   BINDING     218    218       NAD (By similarity).
FT   BINDING     241    241       Substrate (By similarity).
FT   BINDING     263    263       Substrate (By similarity).
FT   BINDING     266    266       Substrate (By similarity).
FT   BINDING     333    333       Substrate (By similarity).
FT   BINDING     366    366       Substrate (By similarity).
FT   BINDING     420    420       Substrate (By similarity).
FT   BINDING     425    425       Substrate (By similarity).
SQ   SEQUENCE   451 AA;  47770 MW;  5A2D5AA7B990ECCF CRC64;
     MLNVTDLRGH TPSKSDIRRA LPRGGTDVVS VLPIVEPVVD DVQNRGAEAA LDYGEKFDHI
     RPASVRVPAE VLKAAEDTLD PRVREAIEES IRRVRKVHAD QKPREHTTEL APGGTVTERF
     LPIDRVGLYV PGGNAVYPSS VIMNAVPAQE AGVGTLVVAS PPQADHGGWP HPTILAACSI
     LGVDEVWAVG GAQAVALLAF GDDSADLEPV DIITGPGNIF VTAAKRLVRG VVGTDSEAGP
     TEIAILADDT ANPVNVAYDL ISQAEHDVMA ASVLITDSEQ LARDVNREIE ARYAITRNAD
     RVAEALRGKQ SGIVLVDDIE VGIAVADQYA AEHLEVHTAN AREVSERISN AGAIFVGDFS
     PVPLGDYSAG SNHVLPTSGT ARFSAGLSTH TFLRPVNLIE YDEAALKDIS EVVINFADAE
     DLPAHGEAIR ARFETLPTTT ADTTDTPDAT A
//