ID   HISX_AQUAE              Reviewed;         426 AA.
AC   O66976;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=aq_782;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06931.1; -; Genomic_DNA.
DR   PIR; E70368; E70368.
DR   RefSeq; NP_213537.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1193426; -.
DR   GenomeReviews; AE000657_GR; aq_782.
DR   KEGG; aae:aq_782; -.
DR   NMPDR; fig|224324.1.peg.552; -.
DR   HOGENOM; O66976; -.
DR   OMA; O66976; LDAHKNA.
DR   BioCyc; AAEO224324:AQ_782-MON; -.
DR   BRENDA; 1.1.1.23; 189781.
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    426       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135717.
FT   ACT_SITE    323    323       Proton acceptor (By similarity).
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   METAL       255    255       Zinc (By similarity).
FT   METAL       258    258       Zinc (By similarity).
FT   METAL       357    357       Zinc (By similarity).
FT   METAL       416    416       Zinc (By similarity).
FT   BINDING     130    130       NAD (By similarity).
FT   BINDING     187    187       NAD (By similarity).
FT   BINDING     210    210       NAD (By similarity).
FT   BINDING     233    233       Substrate (By similarity).
FT   BINDING     255    255       Substrate (By similarity).
FT   BINDING     258    258       Substrate (By similarity).
FT   BINDING     324    324       Substrate (By similarity).
FT   BINDING     357    357       Substrate (By similarity).
FT   BINDING     411    411       Substrate (By similarity).
FT   BINDING     416    416       Substrate (By similarity).
SQ   SEQUENCE   426 AA;  47447 MW;  3F54ED61A772C005 CRC64;
     MRIEDLRKED WKLNERLEYL AKRGEILEEE YEKSVKEILK RVREEGDRAV IEFTKKFDGV
     ELTPENMEVP FEELEKAYEE IEPEVREALE FAENRIRVFH EKQLENSFFK EEEGIILGQK
     VVPLEKVGVY VPGGKAAYPS TVLMNVVPAS VAGVEEIIMV SPKPNKYTLA AAYIAGVSRV
     FQVGGAQAIG ALAYGTEKIP KVDKIVGPGN IYVALAKKLV FGTVDIDMIA GPSEVLVIAD
     ERANPTWVAA DMLSQAEHDE LAASILLTPS EELANKVKEE VERLLSQLER KEIAQKSLEK
     FGTIFLVKDL YHACEVANYI APEHLEVMVR EPMALLPELK HAGAIFLGDY TTEPLGDYVL
     GPNHTLPTGG STRFFSPLGV YDFIKRSSVL YVSREGFKRV ANQAEAIAKA EGLTAHALAV
     KVRKND
//