ID   HISX2_SILPO             Reviewed;         433 AA.
AC   Q5LUS2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Histidinol dehydrogenase 2;
DE            Short=HDH 2;
DE            EC=1.1.1.23;
GN   Name=hisD2; OrderedLocusNames=SPO0981;
OS   Silicibacter pomeroyi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=89184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
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; CP000031; AAV94285.1; -; Genomic_DNA.
DR   RefSeq; YP_166233.1; -.
DR   GeneID; 3193830; -.
DR   GenomeReviews; CP000031_GR; SPO0981.
DR   KEGG; sil:SPO0981; -.
DR   NMPDR; fig|246200.3.peg.1401; -.
DR   HOGENOM; Q5LUS2; -.
DR   OMA; Q5LUS2; NVGCYVP.
DR   BioCyc; SPOM246200:SPO_0981-MON; -.
DR   BRENDA; 1.1.1.23; 278247.
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 2.
FT                                /FTId=PRO_0000135847.
FT   ACT_SITE    319    319       Proton acceptor (By similarity).
FT   ACT_SITE    320    320       Proton acceptor (By similarity).
FT   METAL       249    249       Zinc (By similarity).
FT   METAL       252    252       Zinc (By similarity).
FT   METAL       353    353       Zinc (By similarity).
FT   METAL       412    412       Zinc (By similarity).
FT   BINDING     119    119       NAD (By similarity).
FT   BINDING     181    181       NAD (By similarity).
FT   BINDING     204    204       NAD (By similarity).
FT   BINDING     227    227       Substrate (By similarity).
FT   BINDING     249    249       Substrate (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
FT   BINDING     320    320       Substrate (By similarity).
FT   BINDING     353    353       Substrate (By similarity).
FT   BINDING     407    407       Substrate (By similarity).
FT   BINDING     412    412       Substrate (By similarity).
SQ   SEQUENCE   433 AA;  45353 MW;  B67DC5531FADA3A3 CRC64;
     MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS GEIVVSPDQV
     ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL RPGLIAGQKQ IPLAAAGAYV
     PGGRYAHIAS ALMSIATARA AGVGQITAVS PPQVGRGVHP AILYAMSLAG ADRILALGGV
     QGVAALAFGL FGAPPADILV GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL
     TVAWDLVGQA EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV
     ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA FGDKASGPNH
     VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT ATISRAEGME GHARTADIRL
     EKLRPTLRQV GTG
//