ID   HISX1_RALEJ             Reviewed;         445 AA.
AC   Q46WL2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Histidinol dehydrogenase 1;
DE            Short=HDH 1;
DE            EC=1.1.1.23;
GN   Name=hisD1; OrderedLocusNames=Reut_A3111;
OS   Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000090; AAZ62471.1; -; Genomic_DNA.
DR   RefSeq; YP_297315.1; -.
DR   GeneID; 3611937; -.
DR   GenomeReviews; CP000090_GR; Reut_A3111.
DR   KEGG; reu:Reut_A3111; -.
DR   NMPDR; fig|264198.3.peg.3551; -.
DR   HOGENOM; Q46WL2; -.
DR   OMA; Q46WL2; LDAHKNA.
DR   BioCyc; REUT264198:REUT_A3111-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    445       Histidinol dehydrogenase 1.
FT                                /FTId=PRO_0000135826.
FT   ACT_SITE    341    341       Proton acceptor (By similarity).
FT   ACT_SITE    342    342       Proton acceptor (By similarity).
FT   METAL       273    273       Zinc (By similarity).
FT   METAL       276    276       Zinc (By similarity).
FT   METAL       375    375       Zinc (By similarity).
FT   METAL       434    434       Zinc (By similarity).
FT   BINDING     144    144       NAD (By similarity).
FT   BINDING     205    205       NAD (By similarity).
FT   BINDING     228    228       NAD (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
FT   BINDING     273    273       Substrate (By similarity).
FT   BINDING     276    276       Substrate (By similarity).
FT   BINDING     342    342       Substrate (By similarity).
FT   BINDING     375    375       Substrate (By similarity).
FT   BINDING     429    429       Substrate (By similarity).
FT   BINDING     434    434       Substrate (By similarity).
SQ   SEQUENCE   445 AA;  47888 MW;  4E3DF54A378ADE4B CRC64;
     MNATEMENVS IRRLDSSDPR FAQALREVLA FEAGEDEAID RAVAQILADV KDRGDAAVLE
     YTQRFDRVEA ASMGALEISQ SELEAALEDL EPKRRAALEA AAARVRAYHE KQKIECGSHS
     WEYTEADGTM LGQKVTPLDR VGIYVPGGKA AYPSSVLMNA IPARVAGVKE IIMVVPTPGG
     VRNELVLAAA QIAGVDRVFT IGGAQAVGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG
     TVGIDMIAGP SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAD YIAQVEASIQ
     RQLDSMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP RQWSEKIRHA
     GAIFLGRYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD FQKRSSLIEV SEGGAQMLGQ
     IAAELAYGEG LQAHARSAEY RFKRS
//