ID   HISX_BRUSU              Reviewed;         430 AA.
AC   Q8G2R2;
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=BR0252;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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; AE014291; AAN29201.1; -; Genomic_DNA.
DR   RefSeq; NP_697286.1; -.
DR   HSSP; P06988; 1KAE.
DR   GeneID; 1165911; -.
DR   GenomeReviews; AE014291_GR; BR0252.
DR   KEGG; bms:BR0252; -.
DR   NMPDR; fig|204722.1.peg.243; -.
DR   TIGR; BR0252; -.
DR   HOGENOM; Q8G2R2; -.
DR   OMA; Q8G2R2; LLPEMPR.
DR   BioCyc; BSUI204722:BR_0252-MON; -.
DR   BRENDA; 1.1.1.23; 281610.
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    430       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135741.
FT   ACT_SITE    327    327       Proton acceptor (By similarity).
FT   ACT_SITE    328    328       Proton acceptor (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       262    262       Zinc (By similarity).
FT   METAL       361    361       Zinc (By similarity).
FT   METAL       420    420       Zinc (By similarity).
FT   BINDING     130    130       NAD (By similarity).
FT   BINDING     191    191       NAD (By similarity).
FT   BINDING     214    214       NAD (By similarity).
FT   BINDING     237    237       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     328    328       Substrate (By similarity).
FT   BINDING     361    361       Substrate (By similarity).
FT   BINDING     415    415       Substrate (By similarity).
FT   BINDING     420    420       Substrate (By similarity).
SQ   SEQUENCE   430 AA;  46072 MW;  2752FA59731001E0 CRC64;
     MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL DYSRRFDRID
     LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA RQLPKDDRYT DALGVELGSR
     WTAIEAVGLY VPGGTASYPS SVLMNAMPAK VAGVDRIVMV VPAPDGNLNP LVLVAARLAG
     VSEIYRVGGA QAIAALAYGT ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL
     IVADKDNNPD WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA
     SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF IGGYTPEVIG
     DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ LRALGPAAIE IARAEGLDAH
     AQSVAIRLNL
//