ID   HISX_BACTN              Reviewed;         428 AA.
AC   Q8ABA9;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=BT_0201;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; AE015928; AAO75308.1; -; Genomic_DNA.
DR   RefSeq; NP_809114.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1074912; -.
DR   GenomeReviews; AE015928_GR; BT_0201.
DR   KEGG; bth:BT_0201; -.
DR   NMPDR; fig|226186.1.peg.201; -.
DR   HOGENOM; Q8ABA9; -.
DR   OMA; Q8ABA9; LDAHKNA.
DR   BioCyc; BTHE226186:BT_0201-MON; -.
DR   BRENDA; 1.1.1.23; 21018.
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    428       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135732.
FT   ACT_SITE    323    323       Proton acceptor (By similarity).
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   METAL       256    256       Zinc (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       357    357       Zinc (By similarity).
FT   METAL       416    416       Zinc (By similarity).
FT   BINDING     125    125       NAD (By similarity).
FT   BINDING     187    187       NAD (By similarity).
FT   BINDING     210    210       NAD (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       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   428 AA;  46246 MW;  3C7BEEFF3BA154D1 CRC64;
     MMKLIKYPSK EQWAELLKRP ALNTESLFDT VRTIINKVRA EGDKAVLEYE AAFDKVTLSA
     LTVTSEEIQK AEGLISDELK SAITLAKRNI ETFHSSQRFV GKKVETMEGV TCWQKAVGIE
     KVGLYIPGGT APLFSTVLML AVPAKIAGCR EIVLCTPPDK NGNIHPAILF AAQLAGVSKI
     FKAGGVQAIA AMAYGTESVP KVYKIFGPGN QYVTAAKQLV SLRDVAIDMP AGPSEVEVLA
     DASANPVFVA ADLLSQAEHG VDSQAMLITT SEKLQAEVME EVNRQLAKLP RREIAAKSLE
     NSKLILVKDM DEALELTNAY APEHLIVETE NYLEVAERVI NAGSVFLGSL TPESAGDYAS
     GTNHTLPTNG YAKAYSGVSL DSFIRKITFQ EILPQGMKVI GPAIEEMAAN ELLDAHKNAV
     TVRLNTLK
//