ID   HISX2_RHOS4             Reviewed;         441 AA.
AC   Q3J4H6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   04-NOV-2008, entry version 22.
DE   RecName: Full=Putative histidinol dehydrogenase 2;
DE            Short=HDH 2;
DE            EC=1.1.1.23;
GN   Name=hisD2; OrderedLocusNames=RHOS4_07400; ORFNames=RSP_2155;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
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., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-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   -!- 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   -!- CAUTION: Could lack activity as the potential substrate and zinc-
CC       binding sites are missing.
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DR   EMBL; CP000143; ABA78308.1; -; Genomic_DNA.
DR   RefSeq; YP_352209.1; -.
DR   GeneID; 3719625; -.
DR   GenomeReviews; CP000143_GR; RHOS4_07400.
DR   KEGG; rsp:RSP_2155; -.
DR   NMPDR; fig|272943.3.peg.1346; -.
DR   HOGENOM; Q3J4H6; -.
DR   BioCyc; RSPH272943:RSP_2155-MON; -.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
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_DHase.
DR   InterPro; IPR012131; Hstdl_DHase_prok.
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    441       Putative histidinol dehydrogenase 2.
FT                                /FTId=PRO_0000229864.
FT   ACT_SITE    334    334       Proton acceptor (By similarity).
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
SQ   SEQUENCE   441 AA;  46882 MW;  B1481F195AAEA18E CRC64;
     MVQVNFQVLA ELDAAGRAAL LRRSETDLSM FLEKVGPILE AVRTEGDAAL VRFGRELDRA
     EGLTREGLKV TEAEFDEAFG LVEPEIVAAI RFAIGNIRTF HEEQAPEPMW LKELRPGAFA
     GDRFTPIRSV ALYVPRGKGS FPSVTMMTSV PAVVAKVPQI AIFTPPAPDG RVDAATLVAA
     RLAGVETVYK VGGAQAVAAA AYGTETVTPA LKIVGPGSPW VVAAKRLLAG VIDPGLPAGP
     SESIILADET VHGGLAALDL LIEAEHGPDS SAWLVTHSRQ VAEEALAALP GHWSAMTPQR
     VDFSQAVLCG RAGGIVLTGS AEESHAFVND YAPEHLQILS EKPFEHLGRI TEAAEVLMGP
     HTPITIANFC LGPNAVLPTS RGARTWGPLS VHDFLRRSSV GYVTAPAYPE LAEVAKRLAE
     YEGFSSHANA VGPMRDAYLK R
//