ID   HISX_BURM1              Reviewed;         438 AA.
AC   Q845V3; A9AE01;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-NOV-2008, entry version 37.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=Bmul_0328, BMULJ_02926;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22638290; PubMed=12754231;
RX   DOI=10.1128/JB.185.11.3333-3343.2003;
RA   Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT   "Distribution and organization of auxotrophic genes on the
RT   multichromosomal genome of Burkholderia multivorans ATCC 17616.";
RL   J. Bacteriol. 185:3333-3343(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S.,
RA   Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M.,
RA   Yuji N., Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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.
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DR   EMBL; AB091436; BAC65270.1; -; Genomic_DNA.
DR   EMBL; CP000868; ABX14023.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44811.1; -; Genomic_DNA.
DR   RefSeq; YP_001578520.1; -.
DR   RefSeq; YP_001947347.1; -.
DR   GeneID; 5765433; -.
DR   GeneID; 6359505; -.
DR   GenomeReviews; CP000868_GR; Bmul_0328.
DR   GenomeReviews; AP009385_GR; BMULJ_02926.
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   InterPro; IPR002035; VWF_A.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   PRINTS; PR00453; VWFADOMAIN.
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    438       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135749.
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
FT   ACT_SITE    336    336       Proton acceptor (By similarity).
FT   METAL       267    267       Zinc (By similarity).
FT   METAL       270    270       Zinc (By similarity).
FT   METAL       369    369       Zinc (By similarity).
FT   METAL       428    428       Zinc (By similarity).
FT   BINDING     138    138       NAD (By similarity).
FT   BINDING     199    199       NAD (By similarity).
FT   BINDING     222    222       NAD (By similarity).
FT   BINDING     245    245       Substrate (By similarity).
FT   BINDING     267    267       Substrate (By similarity).
FT   BINDING     270    270       Substrate (By similarity).
FT   BINDING     336    336       Substrate (By similarity).
FT   BINDING     369    369       Substrate (By similarity).
FT   BINDING     423    423       Substrate (By similarity).
FT   BINDING     428    428       Substrate (By similarity).
FT   CONFLICT     90    101       AALEAAAARVRG -> GRAGSGCRTRAR (in Ref. 1;
FT                                BAC65270).
SQ   SEQUENCE   438 AA;  46515 MW;  8F702C8C7E014B1D CRC64;
     MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA AVLEYTNRFD
     RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR GYHEKQKIEC GTHSWQYTES
     DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGVKNDLV
     LAAALLGGVD RVFTIGGAQA VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM
     IAGPSEILVL CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM
     PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ IRHAGAIFLG
     RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS LIEVSAEGAH TLGEIAAELA
     YGEGLQAHAK SAEFRMKG
//