ID   HISX_CAMJE              Reviewed;         428 AA.
AC   Q9PM77; Q0P830;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=Cj1598;
OS   Campylobacter jejuni.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11168 / Serotype O:2;
RX   MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35695.1; -; Genomic_DNA.
DR   PIR; D81255; D81255.
DR   HSSP; P06988; 1K75.
DR   GenomeReviews; AL111168_GR; Cj1598.
DR   KEGG; cje:Cj1598; -.
DR   BioCyc; CJEJ192222:CJ1598-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    428       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135751.
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     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;  46446 MW;  16F08561BF7DB738 CRC64;
     MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDKALIE QALKFDKAEI
     SKIKITQEEI TQASNRLDKD LQEAILVAYE NIKKFHEAQI PHEIALETTK GVKCEVLTRP
     IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG CEKIVLASPA KINDAVLFCA KLCGVDEIYQ
     MGGAGAIAAL TYGTQSVLKV DKIFGPGNAF VTEAKRQVSS DINGAAIDMQ AGPSEVLVIA
     DDLANEKFVA SDLLSQAEHG ADSQVILVCL SQDFAKKASD EVQSQLELLP RKELASKSIA
     NSRIIIAKDL NQALEISNLY APEHLIIQTQ NPRELLKGVK HAGSVFLGAY SPESMGDYAS
     GTNHVLPTYG LTKTHSSLGL ADFSKRMTVQ ELSKEGFLAL GKSVEILAQN EHLDAHKNAV
     TFRLESLK
//