ID   HISX2_PELUB             Reviewed;         428 AA.
AC   Q4FMH0;
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 2;
DE            Short=HDH 2;
DE            EC=1.1.1.23;
GN   Name=hisD2; OrderedLocusNames=SAR11_0801;
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; AAZ21619.1; -; Genomic_DNA.
DR   RefSeq; YP_266222.1; -.
DR   GeneID; 3516715; -.
DR   GenomeReviews; CP000084_GR; SAR11_0801.
DR   KEGG; pub:SAR11_0801; -.
DR   HOGENOM; Q4FMH0; -.
DR   OMA; Q4FMH0; CYGSLFL.
DR   BioCyc; CPEL335992:SAR11_0801-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 2.
FT                                /FTId=PRO_0000135810.
FT   ACT_SITE    320    320       Proton acceptor (By similarity).
FT   ACT_SITE    321    321       Proton acceptor (By similarity).
FT   METAL       250    250       Zinc (By similarity).
FT   METAL       253    253       Zinc (By similarity).
FT   METAL       354    354       Zinc (By similarity).
FT   METAL       413    413       Zinc (By similarity).
FT   BINDING     228    228       Substrate (By similarity).
FT   BINDING     250    250       Substrate (By similarity).
FT   BINDING     253    253       Substrate (By similarity).
FT   BINDING     321    321       Substrate (By similarity).
FT   BINDING     354    354       Substrate (By similarity).
FT   BINDING     408    408       Substrate (By similarity).
FT   BINDING     413    413       Substrate (By similarity).
SQ   SEQUENCE   428 AA;  46658 MW;  0DE1C63534A76B41 CRC64;
     MAITYLKKSP KTSSTDDTKT TGIVQDLLKN IETTKEQGCI DLTKKFDKYD GEIIVSKERI
     EEIKKTLDQK TKDDVQFSYE RVRKFAEAQL KNYGQDFEVE LSDGLFAGQK LIPVNTAGCY
     VPGGRYAHIA SAVMSVTTAK VAGVKNVIAC SPPKEGVGAH PTIIYTADLC GADVILNLGG
     VPAIAAMTNG LFNNPPADII VGPGNQFVAE AKRILFGKVG IDLFAGPTEI GIIADAKADP
     EIVAVDLVGQ AEHGYNSPCW LYTTSKELAE KVMKRVPELI AELPEVPRTN ADAAWRDYGE
     VILCDTDEEM ATISDEYAPE HLEVQTENLE WFHKRLTNYG SLFIGEETTV AYGDKCSGTN
     HILPTKGAGR YTGGLFVGKF VKTLSFQRMT KESTELVGAA AARISRYEGM EAHARTGDVR
     LKKYGYSS
//