ID   HISX2_ANAVT             Reviewed;         433 AA.
AC   Q3M5D3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Histidinol dehydrogenase 2;
DE            Short=HDH 2;
DE            EC=1.1.1.23;
GN   Name=hisD2; OrderedLocusNames=Ava_4204;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
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., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
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   -!- 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000117; ABA23803.1; -; Genomic_DNA.
DR   RefSeq; YP_324698.1; -.
DR   GeneID; 3680948; -.
DR   GenomeReviews; CP000117_GR; Ava_4204.
DR   KEGG; ava:Ava_4204; -.
DR   NMPDR; fig|240292.3.peg.4200; -.
DR   HOGENOM; Q3M5D3; -.
DR   OMA; Q3M5D3; LGVETFM.
DR   BioCyc; AVAR240292:AVA_4204-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    433       Histidinol dehydrogenase 2.
FT                                /FTId=PRO_0000229849.
FT   ACT_SITE    328    328       Proton acceptor (By similarity).
FT   ACT_SITE    329    329       Proton acceptor (By similarity).
FT   METAL       260    260       Zinc (By similarity).
FT   METAL       263    263       Zinc (By similarity).
FT   METAL       362    362       Zinc (By similarity).
FT   METAL       421    421       Zinc (By similarity).
FT   BINDING     130    130       NAD (By similarity).
FT   BINDING     192    192       NAD (By similarity).
FT   BINDING     215    215       NAD (By similarity).
FT   BINDING     238    238       Substrate (By similarity).
FT   BINDING     260    260       Substrate (By similarity).
FT   BINDING     263    263       Substrate (By similarity).
FT   BINDING     329    329       Substrate (By similarity).
FT   BINDING     362    362       Substrate (By similarity).
FT   BINDING     416    416       Substrate (By similarity).
FT   BINDING     421    421       Substrate (By similarity).
SQ   SEQUENCE   433 AA;  46701 MW;  5C294698068A3ABA CRC64;
     MLRIITQQAD VKAELQRICD RTHDEQVLHK EATVREVLQA VKRQGDKAVL HYTDEFDNQI
     LKAEELRVTG SELDAAYQQV SKELLEAIQL ASRQIEAFHR QRVPKSWVHF GDDDIVLGKR
     YTPVDRAGLY VPGGRAAYVS TVLMNAIPAK VAGVPRIVMA TPPGAQKAIN PAVLVAAQEV
     GVQEIYRVGG AQAIAALAYG TETIPKVDVI TGPGNIYVTL AKKLVYGTVG IDSLAGPSEV
     LIIADEGANP VHVATDMLAQ AEHDPMAAAI LFTTDPALAK NVQVAVERQL VDHPRRIDTE
     KAIAHYGLIV LVESLDAAAE LSNEFAPEHL ELEVKDPWAV LPNIRHAGAI FLGYSTPEAV
     GDYLAGPNHT LPTSGAARYA SALSVETFLK HSSIIQYSQT ALNKVAGAID ALATAEGLPS
     HADSVKRRIQ QDE
//