ID   HISX_BUCBP              Reviewed;         435 AA.
AC   P59398;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 1.
DT   25-NOV-2008, entry version 46.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=bbp_094;
OS   Buchnera aphidicola subsp. Baizongia pistaciae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=135842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; AE016826; AAO26829.1; -; Genomic_DNA.
DR   RefSeq; NP_777724.1; -.
DR   HSSP; P06988; 1KAE.
DR   GeneID; 1058171; -.
DR   GenomeReviews; AE016826_GR; bbp_094.
DR   KEGG; bab:bbp094; -.
DR   HOGENOM; P59398; -.
DR   BioCyc; BAPH224915:BBP_094-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    435       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135743.
FT   ACT_SITE    327    327       Proton acceptor (By similarity).
FT   ACT_SITE    328    328       Proton acceptor (By similarity).
FT   METAL       260    260       Zinc (By similarity).
FT   METAL       263    263       Zinc (By similarity).
FT   METAL       361    361       Zinc (By similarity).
FT   METAL       420    420       Zinc (By similarity).
FT   BINDING     131    131       NAD (By similarity).
FT   BINDING     189    189       NAD (By similarity).
FT   BINDING     212    212       NAD (By similarity).
FT   BINDING     238    238       Substrate (By similarity).
FT   BINDING     260    260       Substrate (By similarity).
FT   BINDING     263    263       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   435 AA;  48185 MW;  8A2F3ED2073D73F2 CRC64;
     MEVYIPIIYW KSCSEKEKRE ILFRPVVNDN SQIKEVVKEI ITNVKNSGDK ALYDYTKTFD
     KIRLESIQVS YGEIVDSDSF VNEEIQKSIS VAKNNIKIFH EKQTHNVVNI EIQPGVFCRQ
     IIRPIQSVGL YIPGGCAPLV STVLMLAIPA KIVGCKNIIL CSPPPITKEI LYASKICGIH
     NIFQVGGAQA IAAMAFGTKT IPKVNKIFGP GNVYVTEAKL QINALLNDLS IDMLAGPSEI
     LIIADFKANA CIIASDFLSQ MEHGIYSQAI LVTPSYDLAC NVIFEINIQL KNLSRKKVIN
     KSLKYSRIIV TKTLLECFEI SNLYAPEHLI IQCENSNRLL VYVINAGSIF LGRWSAVASG
     DYVTGTNHVL PTYGSAIVNS GLTVMDFQKI ISVQKLDQQG LIDVSSSIIS LSEVERMDAH
     TNSIKQRLIA LQDVK
//