ID   HISX_DEHE1              Reviewed;         436 AA.
AC   Q3Z878;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=DET0844;
OS   Dehalococcoides ethenogenes (strain 195).
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M.,
RA   Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M.,
RA   Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M.,
RA   Sullivan S.A., Madupu R., Nelson K.E., Kang K.H., Impraim M., Tran K.,
RA   Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H.,
RA   Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(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; CP000027; AAW39898.1; -; Genomic_DNA.
DR   RefSeq; YP_181571.1; -.
DR   GeneID; 3229860; -.
DR   GenomeReviews; CP000027_GR; DET0844.
DR   KEGG; det:DET0844; -.
DR   NMPDR; fig|243164.3.peg.943; -.
DR   TIGR; DET0844; -.
DR   HOGENOM; Q3Z878; -.
DR   OMA; Q3Z878; LGVETFM.
DR   BioCyc; DETH243164:DET_0844-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    436       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135764.
FT   ACT_SITE    334    334       Proton acceptor (By similarity).
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
FT   METAL       266    266       Zinc (By similarity).
FT   METAL       269    269       Zinc (By similarity).
FT   METAL       368    368       Zinc (By similarity).
FT   METAL       427    427       Zinc (By similarity).
FT   BINDING     136    136       NAD (By similarity).
FT   BINDING     198    198       NAD (By similarity).
FT   BINDING     221    221       NAD (By similarity).
FT   BINDING     244    244       Substrate (By similarity).
FT   BINDING     266    266       Substrate (By similarity).
FT   BINDING     269    269       Substrate (By similarity).
FT   BINDING     335    335       Substrate (By similarity).
FT   BINDING     368    368       Substrate (By similarity).
FT   BINDING     422    422       Substrate (By similarity).
FT   BINDING     427    427       Substrate (By similarity).
SQ   SEQUENCE   436 AA;  46836 MW;  B5BDCD65764EA53F CRC64;
     MEIIRGFAPA EKRLSRRDKA GFFLDETQRA ELAKRLGVDP EKAVNGIIDD IRKQGDKAVL
     EYTLKFDRAA ISKLEVSPAE IKQAAGEIPA ELFEALKLAA TQVRAYHHFQ KEAVWKAAEI
     MQGKQLIRPL ERVGLYVPGG KAFYPSTVLM TAIPAKEAGV DEIILVTPPG ADGKIPAPTL
     AAAYIAGVDK VFACGGAQAV AALAFGTKSI PKVDKICGPG NIFVTLAKKA VFGVVDIDGL
     QGPSEVLILA DQYANAEYCA SDILAQAEHD VLASPIMVTT SAELAKRVND IVETKAGSCA
     RKDIIRQSLR DNGLIAVVDN MDEAIKLANM YATEHLCLLV KDSEQYLSRI NHAGCIFYGE
     KASVVMGDYV AGPSHALPTS GTARFSSPLN ILDFVKYIDI VNVSKEEVTK LGKAAVTIAR
     AEGLECHAEA ALKRME
//