ID   HISX_BIFLO              Reviewed;         471 AA.
AC   Q8G4S9;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=BL1295;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN25096.1; -; Genomic_DNA.
DR   RefSeq; NP_696460.1; -.
DR   HSSP; P06988; 1KAE.
DR   GeneID; 1022774; -.
DR   GenomeReviews; AE014295_GR; BL1295.
DR   KEGG; blo:BL1295; -.
DR   NMPDR; fig|206672.1.peg.1227; -.
DR   HOGENOM; Q8G4S9; -.
DR   OMA; Q8G4S9; LDAHKNA.
DR   BioCyc; BLON206672:BL1295-MON; -.
DR   BRENDA; 1.1.1.23; 39917.
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    471       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135733.
FT   ACT_SITE    350    350       Proton acceptor (By similarity).
FT   ACT_SITE    351    351       Proton acceptor (By similarity).
FT   METAL       281    281       Zinc (By similarity).
FT   METAL       284    284       Zinc (By similarity).
FT   METAL       384    384       Zinc (By similarity).
FT   METAL       443    443       Zinc (By similarity).
FT   BINDING     139    139       NAD (By similarity).
FT   BINDING     204    204       NAD (By similarity).
FT   BINDING     236    236       NAD (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     281    281       Substrate (By similarity).
FT   BINDING     284    284       Substrate (By similarity).
FT   BINDING     351    351       Substrate (By similarity).
FT   BINDING     384    384       Substrate (By similarity).
FT   BINDING     438    438       Substrate (By similarity).
FT   BINDING     443    443       Substrate (By similarity).
SQ   SEQUENCE   471 AA;  50257 MW;  36D6D724978BDC88 CRC64;
     MLRWGVMSEN IMRIIDLRGQ NLSRAELLAA MPRAAMGTSE ATDLVRPILD DVKERGAAAL
     RDFEEKFDHV RPKNLRVPVE AIKDALTTLD PEVRAAIEES VRRARAVAAN QVPKDFYTDL
     AEGARVAERW IPIQRVGLYV PGGKAVYPSS VIMNAVPAQA AGVESLAIAT PPARDNEEGL
     PNKTILATCA ILGVDEVYAV GGAQAIAMFA YGAKGSEPQD GDILCDPVDK ITGPGNIFVA
     TAKSLVSAFV GIDAVAGPTE IGIIADETAN PSLLAADLIG QAEHDELAGS VLFTDSTEIA
     DKVQESLKYR VPRTEHAERV HTSLSGTQSA IVLTDGLDQS IDAANAYAAE HLEIQTKDAD
     AVVKRIKNAG AIFRGPYSPV PLGDYMSGSN HVLPTGGTAR FAAGLGVHTF MKPVEVIEYD
     EEGLKALAAR INAFAVSEDL PAHGECVLSR FVKDPYDKAT LREQEKEAGL R
//