ID   HISX2_RALEJ             Reviewed;         436 AA.
AC   Q46N53;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=Reut_C6092;
OS   Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus).
OG   Plasmid megaplasmid Reut.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Vergez L.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of a megaplasmid of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000092; AAZ65418.1; -; Genomic_DNA.
DR   RefSeq; YP_293275.1; -.
DR   GeneID; 3607398; -.
DR   GenomeReviews; CP000092_GR; Reut_C6092.
DR   KEGG; reu:Reut_C6092; -.
DR   NMPDR; fig|264198.3.peg.6; -.
DR   HOGENOM; Q46N53; -.
DR   OMA; Q46N53; CYGSLFL.
DR   BioCyc; REUT264198:REUT_C6092-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; Plasmid; Zinc.
FT   CHAIN         1    436       Histidinol dehydrogenase 2.
FT                                /FTId=PRO_0000135827.
FT   ACT_SITE    318    318       Proton acceptor (By similarity).
FT   ACT_SITE    319    319       Proton acceptor (By similarity).
FT   METAL       248    248       Zinc (By similarity).
FT   METAL       251    251       Zinc (By similarity).
FT   METAL       352    352       Zinc (By similarity).
FT   METAL       411    411       Zinc (By similarity).
FT   BINDING     118    118       NAD (By similarity).
FT   BINDING     180    180       NAD (By similarity).
FT   BINDING     203    203       NAD (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   BINDING     248    248       Substrate (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
FT   BINDING     319    319       Substrate (By similarity).
FT   BINDING     352    352       Substrate (By similarity).
FT   BINDING     406    406       Substrate (By similarity).
FT   BINDING     411    411       Substrate (By similarity).
SQ   SEQUENCE   436 AA;  46881 MW;  E505337929A7046C CRC64;
     MISYLKKAEK TPQTETATAQ KVVTEMLAEI QARGKDAVRQ YAKQLDGWSG DIVLTPDQIR
     EQTKDVPAGV RADIDFAIRQ VTDFALAQRE SLKEFSVELH PGVTAGQRVL PVNVVGCYAP
     AGRYAHIASA YMGVATAKAA GVKTVVACSS PFRGQGIHPH VLYAFQAAGA DVIMALGGVQ
     AIASMAYGLF TGKPADVVVG PGNKFVAEAK RSLYGQVGID VFAGPSEVAV IADETADPAI
     VASDLVGQAE HGHESPAWLF TTSRDLADRV MALVPELIAK LPPTARDAAT AAWRDYGEVI
     LCGTREEVVE ISDRYASEHL EVHTADLDWW LANLTCYGSL FLGEETTVAF GDKTSGPNHV
     LPTKGAARYS GGLSVHKFMK TLTWQQMTRE ATRQIGQVTA RISRLEGMEA HARTADDRMA
     KYFPNASFEM GTPVEV
//