ID   HISX_BRAJA              Reviewed;         431 AA.
AC   P59397;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 1.
DT   25-NOV-2008, entry version 41.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=blr1256;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC46521.1; -; Genomic_DNA.
DR   RefSeq; NP_767896.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1049433; -.
DR   GenomeReviews; BA000040_GR; blr1256.
DR   KEGG; bja:blr1256; -.
DR   NMPDR; fig|224911.1.peg.1256; -.
DR   HOGENOM; P59397; -.
DR   BioCyc; BJAP224911:BLR1256-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    431       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135739.
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   431 AA;  44907 MW;  6FBB4505AD936B6D CRC64;
     MPVRLDRSSA DFDQRFAAFL AAKREVSADV EAAARAIVDD VARRGDAALL EATAKFDRLT
     LDASGLRVSA AEIEAAVKAC DAATLDALSL ARDRIETYHR RQLPKDERFT DPLGVELGWR
     YTAIESAGLY VPGGTAAYPS SVLMNAVPAK VAGVSRLVMV VPSPDGKLNP LVLAAARLGG
     VTEIYRVGGA QAVAALAHGT ATIAPVAKIV GPGNAYVAAA KRLVFGKVGI DMIAGPSEVL
     VIADDTGNAD WIAADLLAQA EHDTSAQSIL ITDSARLAAD VEKAVEAQLK TLPRTAIASA
     SWADFGAIIM VKNLNDAIPL ADAIAAEHLE IMTTDPDALA ARIRNAGAVF LGAHTPEAIG
     DYVGGSNHVL PTARSARFSS GLSVHDFMKR TSILKCGPDQ LRALGPAAMT LGKAEGLDAH
     SRSIGLRLNL S
//