ID   HISX_DECAR              Reviewed;         433 AA.
AC   Q47AL5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=Daro_3387;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000089; AAZ48116.1; -; Genomic_DNA.
DR   RefSeq; YP_286586.1; -.
DR   GeneID; 3567117; -.
DR   GenomeReviews; CP000089_GR; Daro_3387.
DR   KEGG; dar:Daro_3387; -.
DR   NMPDR; fig|159087.4.peg.3635; -.
DR   HOGENOM; Q47AL5; -.
DR   OMA; Q47AL5; LDAHKNA.
DR   BioCyc; DARO159087:DARO_3387-MON; -.
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    433       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135763.
FT   ACT_SITE    330    330       Proton acceptor (By similarity).
FT   ACT_SITE    331    331       Proton acceptor (By similarity).
FT   METAL       262    262       Zinc (By similarity).
FT   METAL       265    265       Zinc (By similarity).
FT   METAL       364    364       Zinc (By similarity).
FT   METAL       423    423       Zinc (By similarity).
FT   BINDING     133    133       NAD (By similarity).
FT   BINDING     194    194       NAD (By similarity).
FT   BINDING     217    217       NAD (By similarity).
FT   BINDING     240    240       Substrate (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     265    265       Substrate (By similarity).
FT   BINDING     331    331       Substrate (By similarity).
FT   BINDING     364    364       Substrate (By similarity).
FT   BINDING     418    418       Substrate (By similarity).
FT   BINDING     423    423       Substrate (By similarity).
SQ   SEQUENCE   433 AA;  46066 MW;  A7E2E5E5990A7CCA CRC64;
     MVAIKRLATV DADFKAQMDA LLAFEAAQDE GIERTVIGIL ADVKARGDAA VVEYSNKFDR
     LTASSMADLE LSKAEMQKAL DGLPADQRQA LEAAAHRVRV YHEKQRMEGW SYTEADGTML
     GQMITPLDRV GLYVPGGKAA YPSSVLMNAI PAKVAGVKEL IMVVPTPGGE HNQLVLAAAC
     LAGVDRVFTI GGAQAVGALA YGTEAVPQVD KIVGPGNAYV ACAKRRVFGI VGIDMIAGPS
     EILVVADGSS DPDWVAMDLF SQAEHDELAQ SILICTDAAY IDRVQASIEK LLPTMPRREV
     IETSLTNRGA LILVRDLEEA CAIANRVAPE HLELSLADPD PWVAKIHHAG AIFIGHYTSE
     SLGDYCAGPN HVLPTSGSAR FSSPLGVYDF QKRTSLIKVS KAGAQTLGKI ASTLAHGEGL
     PAHAKSAEFR LEN
//