ID   HISX_CORJK              Reviewed;         450 AA.
AC   Q4JW59;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=jk0786;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(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   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; CR931997; CAI36948.1; -; Genomic_DNA.
DR   RefSeq; YP_250566.1; -.
DR   GeneID; 3433179; -.
DR   GenomeReviews; CR931997_GR; jk0786.
DR   KEGG; cjk:jk0786; -.
DR   NMPDR; fig|306537.3.peg.1760; -.
DR   HOGENOM; Q4JW59; -.
DR   OMA; Q4JW59; LDAHKNA.
DR   BioCyc; CJEI306537:JK0786-MON; -.
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    450       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135762.
FT   ACT_SITE    339    339       Proton acceptor (By similarity).
FT   ACT_SITE    340    340       Proton acceptor (By similarity).
FT   METAL       270    270       Zinc (By similarity).
FT   METAL       273    273       Zinc (By similarity).
FT   METAL       373    373       Zinc (By similarity).
FT   METAL       432    432       Zinc (By similarity).
FT   BINDING     135    135       NAD (By similarity).
FT   BINDING     197    197       NAD (By similarity).
FT   BINDING     225    225       NAD (By similarity).
FT   BINDING     248    248       Substrate (By similarity).
FT   BINDING     270    270       Substrate (By similarity).
FT   BINDING     273    273       Substrate (By similarity).
FT   BINDING     340    340       Substrate (By similarity).
FT   BINDING     373    373       Substrate (By similarity).
FT   BINDING     427    427       Substrate (By similarity).
FT   BINDING     432    432       Substrate (By similarity).
SQ   SEQUENCE   450 AA;  46775 MW;  2BED7B5FA2E531C5 CRC64;
     MTSAQLDFSR IDLRGQAPTT AELRHRLPRG GTDVDSVIPT VAPIVDQVRE GGARAALEIG
     QRFDGVTPDS VRVPAEVIDA AVGTLADDVI AALEEAIKRV RAFHSAIRPE DKQVEVAPGG
     IVTERFIPVQ RVGLYAPGGN AVYPSSVIMN VVPAQEAGVE SLVVASPPQE GGWPHPTVLA
     ACKLLGVDEV WAVGGAQAVA LLAHGSTAEG GEELEPVDMV TGPGNIFVTA AKRLCRSVVG
     IDSEAGPTEI AVLADESANA VEIAYDLISQ AEHDTMAASV LITDSEKLAD EVVAEMNERY
     HITENSERVA EALSGQQSGV VLVDDIAAGI RAANAYGAEH LEIHTEDAHG VAAQITNAGA
     IFIGRFSPVP LGDYAAGSNH VLPTSGTARH SSGLSTLTFL KSVHVIDYNE EGLRGVADTV
     ITLSKSEGLP AHGEAISART STANTNGTEV
//