ID   HISX2_COLP3             Reviewed;         446 AA.
AC   Q483H8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Histidinol dehydrogenase 2;
DE            Short=HDH 2;
DE            EC=1.1.1.23;
GN   Name=hisD2; OrderedLocusNames=CPS_2061;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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   -!- 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; CP000083; AAZ25938.1; -; Genomic_DNA.
DR   RefSeq; YP_268789.1; -.
DR   GeneID; 3520186; -.
DR   GenomeReviews; CP000083_GR; CPS_2061.
DR   KEGG; cps:CPS_2061; -.
DR   NMPDR; fig|167879.3.peg.1975; -.
DR   TIGR; CPS_2061; -.
DR   HOGENOM; Q483H8; -.
DR   OMA; Q483H8; EAEHGPD.
DR   BioCyc; CPSY167879:CPS_2061-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: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; atypical; 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   NAD; Oxidoreductase.
FT   CHAIN         1    446       Histidinol dehydrogenase 2.
FT                                /FTId=PRO_0000135758.
FT   ACT_SITE    334    334       Proton acceptor (By similarity).
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
SQ   SEQUENCE   446 AA;  48236 MW;  4B8C883BF8A096FA CRC64;
     MTHKVKIHRL SDLSAEQRNK LLQRTESNLD NFIDIVKPII ENVKLNGDKA LSEYAKKFDK
     AEVSTDQIQV TQAEFDEAFT LVDEEVIQTL SYSIDNIKKF HEAQMPEEMW MKQIRPGCYA
     GDRFTPINAV ACYIPRGKGS FPSVAIMTAV PAIVAGVPTA IIITPPGTDG KVDAATLVVA
     KLVGIDKVFK CGGAQGIAAV AYGTNTVPKC DKVVGPGSPF VVAAKKLLAD IIHPGTPAGP
     SEAIVLADDT ANPKLAALDL LVEAEHGPDS SAFLVTNSKE LAEQAQVAIN EYWQHMDRLR
     VDFSSTVLSG DNGGIVLTST FEEAVDFCND YAAEHLLILS KSPFDHLGKI INAGEILLGE
     NTPISIANYT LGPNAVLPTS MAAKTASPLS VFDYLKSCSI GYLTREGYEE LAPHTYRFAK
     YEGFDAHANA VSHLRDEAIK SEKKIK
//