ID   HISX1_PELUB             Reviewed;         428 AA.
AC   Q4FNE2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Histidinol dehydrogenase 1;
DE            Short=HDH 1;
DE            EC=1.1.1.23;
GN   Name=hisD1; OrderedLocusNames=SAR11_0475;
OS   Pelagibacter ubique.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   SAR11 cluster; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L.,
RA   Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M.,
RA   Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(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; CP000084; AAZ21297.1; -; Genomic_DNA.
DR   RefSeq; YP_265900.1; -.
DR   GeneID; 3517238; -.
DR   GenomeReviews; CP000084_GR; SAR11_0475.
DR   KEGG; pub:SAR11_0475; -.
DR   HOGENOM; Q4FNE2; -.
DR   OMA; Q4FNE2; LDAHKNA.
DR   BioCyc; CPEL335992:SAR11_0475-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    428       Histidinol dehydrogenase 1.
FT                                /FTId=PRO_0000135809.
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   ACT_SITE    325    325       Proton acceptor (By similarity).
FT   METAL       256    256       Zinc (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       358    358       Zinc (By similarity).
FT   METAL       417    417       Zinc (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     325    325       Substrate (By similarity).
FT   BINDING     358    358       Substrate (By similarity).
FT   BINDING     412    412       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
SQ   SEQUENCE   428 AA;  47310 MW;  87F54F17177A8658 CRC64;
     MIKILDSKNK NFDKTLDALL SKRKNKVQLN SVSVIKIIKD VKKNGDKAIL KYEKRFNKNS
     IIAPSIKQIN RAIQSLDQKV KKAIDLAYDR IYKFHSLQKF KNISYTDKLK NKLEYKYVPI
     ESVAIYVPGS TASYPSSVLM NAVPAIVAGV KRLVMVNPGQ KGKQNPAVLY AAKKCKIKEI
     YSIGGPSAIA AVAYGTKKIK KVDKIIGPGN SYVAAAKKEV FGDVGIEGMI AGPSEVTIVC
     DKFSNPEWIA SDLIGQAEHD NLAQCILISK DKSIIKKVNY EIINQLKELP RAVIAKNSLL
     NNGILIYMPS DQKIINTVNK IAPEHLELNT KNYKKVVSKI KNAGSICLGK YAVMAMTDYN
     VGSNHVLPTN SSARYSSGVS VNEFYKRISY INLSKKGIET LGPSVITLAN YEGLVGHAKS
     VEKRIRRK
//