ID   HISX1_COLP3             Reviewed;         434 AA.
AC   Q47XB8;
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=CPS_3890;
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   -!- 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; CP000083; AAZ27302.1; -; Genomic_DNA.
DR   RefSeq; YP_270552.1; -.
DR   GeneID; 3521558; -.
DR   GenomeReviews; CP000083_GR; CPS_3890.
DR   KEGG; cps:CPS_3890; -.
DR   NMPDR; fig|167879.3.peg.3530; -.
DR   TIGR; CPS_3890; -.
DR   HOGENOM; Q47XB8; -.
DR   OMA; Q47XB8; LDAHKNA.
DR   BioCyc; CPSY167879:CPS_3890-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    434       Histidinol dehydrogenase 1.
FT                                /FTId=PRO_0000135757.
FT   ACT_SITE    329    329       Proton acceptor (By similarity).
FT   ACT_SITE    330    330       Proton acceptor (By similarity).
FT   METAL       262    262       Zinc (By similarity).
FT   METAL       265    265       Zinc (By similarity).
FT   METAL       363    363       Zinc (By similarity).
FT   METAL       422    422       Zinc (By similarity).
FT   BINDING     129    129       NAD (By similarity).
FT   BINDING     191    191       NAD (By similarity).
FT   BINDING     214    214       NAD (By similarity).
FT   BINDING     240    240       Substrate (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     265    265       Substrate (By similarity).
FT   BINDING     330    330       Substrate (By similarity).
FT   BINDING     363    363       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
FT   BINDING     422    422       Substrate (By similarity).
SQ   SEQUENCE   434 AA;  45853 MW;  CD2635AFC75E5169 CRC64;
     MINQLINWQE LSPQQKNSAL ARPAIADSAL LSTQVANILS QVKNQGDKAI LALTEQFDGI
     ALSTLSVSSA QVAQAKLALT DKRLKAIHTA YKQIKSFHSA QTASDITVET TPGVKCTLKT
     EAIESVGLYI PAGSAPLPST VLMLGVPAQL TGCQRTVLVC PPDKNGQLAD EILVAADLCG
     ITEIYTVGGA QAIAALAYGT ETIPAVNKVF GPGNRYVTEA KTQLSQQVAG FAIDMPAGPS
     EVLVIADGQA NPAFIAADLL SQAEHGVDSQ VILLSDSESL ISKVSTEIAQ QLTLLSRCKI
     AEQALKQSRL ILTKDLAQAV EVSNEYGPEH LIIQTEDAPT LLSKLRNAGS IFVGAYTPES
     AGDYASGTNH VLPTYGYSKV ISSLSLADFS RRFTVQEITK AGLQSLAECI IELTDAEGLD
     AHQRAVTIRL EEGS
//