ID   HISX_BLOPB              Reviewed;         443 AA.
AC   Q492K3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-NOV-2008, entry version 25.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=BPEN_478;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41094.1; -; Genomic_DNA.
DR   RefSeq; YP_277970.1; -.
DR   GeneID; 3562985; -.
DR   GenomeReviews; CP000016_GR; BPEN_478.
DR   KEGG; bpn:BPEN_478; -.
DR   HOGENOM; Q492K3; -.
DR   BioCyc; CBLO291272:BPEN_478-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    443       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135735.
FT   ACT_SITE    329    329       Proton acceptor (By similarity).
FT   ACT_SITE    330    330       Proton acceptor (By similarity).
FT   METAL       262    262       Zinc (By similarity).
FT   METAL       265    265       Zinc (By similarity).
FT   METAL       363    363       Zinc (By similarity).
FT   METAL       422    422       Zinc (By similarity).
FT   BINDING     133    133       NAD (By similarity).
FT   BINDING     191    191       NAD (By similarity).
FT   BINDING     214    214       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     330    330       Substrate (By similarity).
FT   BINDING     363    363       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
FT   BINDING     422    422       Substrate (By similarity).
SQ   SEQUENCE   443 AA;  49150 MW;  E08D5771184EE9F4 CRC64;
     MISHEHPISI YWNDCSKSEQ KKLLTRPINN KLNDIYINVK NILTKVYNEG DRALFKFNFD
     FDNVQTTQLQ IPTEIIMNSG RNLSNEIKQA IHTAMTNITR FHQAQCYSEI IVETLPGVYC
     QQIIRPLNIV GLYVPGGTAP LLSTVMMLGV PARIAKCKRV ILCSPPPIPD VIIYTAQLCG
     IDEIYQIGGS QSIAAMGFGT ESIPKVDKIF GPGNIWVTEA KRQINLAPNG AAIDMLAGPS
     EILIIADNTA NPIFIAADLL SQSEHGPDSH AILITPYSCI AEKTKKELHK QLKILPRNDI
     VRNVLLNSRM IITNNLMECF SISNSYAPEH LIIQIENASD YLHYITNAGS IFLGNWSPET
     AGDYASGPNH VLPTYGRAVA TSGLGVIDFQ KRMSVQQLTQ NGLLQLSSTI TTLTQIEQLK
     AHEYAITHRI NYIKEQNEHS LLG
//