ID   HISX_CAUCR              Reviewed;         428 AA.
AC   Q9A5V1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=CC_2346;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24317.1; -; Genomic_DNA.
DR   PIR; A87540; A87540.
DR   RefSeq; NP_421149.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 943550; -.
DR   GenomeReviews; AE005673_GR; CC_2346.
DR   KEGG; ccr:CC_2346; -.
DR   NMPDR; fig|190650.1.peg.2329; -.
DR   TIGR; CC_2346; -.
DR   HOGENOM; Q9A5V1; -.
DR   OMA; Q9A5V1; LDAHKNA.
DR   BRENDA; 1.1.1.23; 2191.
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_0000135753.
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     129    129       NAD (By similarity).
FT   BINDING     188    188       NAD (By similarity).
FT   BINDING     211    211       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;  45154 MW;  89F4ECF58D67F2F2 CRC64;
     MRRFLFSDPD FQTAFKAFLD ERRGSPADVD AAVAGVLEAV RTQGIEALLD YSRRFDKVDL
     TAETIRVTAE EIEAGAAETP ADVREAIAFA AARIRAYHSR QRPADQAWTD EAGVELGWRW
     TPLEAVGVYV PGGRAAYPST VLMNAVPAQV AGVDRIAMVT PPGKLQPAVL AAAKEAGVTE
     IWRVGGAQAV AALAYGAGPI QPVDKIVGPG NAYVTAAKRR LYGVVGIDAL AGPSEIVVVA
     DNKNNPDWIA ADLLSQAEHD PAAQSILITD DEAFAAAVEQ AIAERLKTLA TGEDAAASWR
     DHGAVIIAPL DESPALVDAI APEHVEFALD NPERLSDRVR HAGAIFLGRV TPEAIGDYVA
     GSNHVLPTSR AARFQSGLSI YDFIKRTSIV KCDPASFAVL GPHTVALAKA EGLPAHALSA
     SVRLPSGD
//