ID   HIS2_SACBA              Reviewed;         799 AA.
AC   Q12670;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Histidine biosynthesis trifunctional protein;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE              EC=3.5.4.19;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE              EC=3.6.1.31;
DE   Includes:
DE     RecName: Full=Histidinol dehydrogenase;
DE              Short=HDH;
DE              EC=1.1.1.23;
GN   Name=HIS2;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Carlsbergensis;
RA   Porter G.L.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-
CC       phosphoribosyl)-5-((5-
CC       phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5-
CC       phosphoribosyl)-AMP + diphosphate.
CC   -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2
CC       NADH.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC       dehydrogenase family.
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DR   EMBL; U13062; AAA21153.1; -; Genomic_DNA.
DR   PIR; S53349; S53349.
DR   HSSP; P06988; 1K75.
DR   BRENDA; 1.1.1.23; 164752.
DR   BRENDA; 3.5.4.19; 164752.
DR   BRENDA; 3.6.1.31; 164752.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:EC.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016298; Histidine_synth_trifunct.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH_prok-type.
DR   InterPro; IPR002496; PRA_CycHdrlase.
DR   InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   PIRSF; PIRSF001257; His_trifunctional; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   ProDom; PD002680; Histidinol_dh; 1.
DR   ProDom; PD002610; PRA_cyclohydro; 1.
DR   ProDom; PD002611; Pra_PH/CH; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis;
KW   Hydrolase; Metal-binding; Multifunctional enzyme; NAD;
KW   Nucleotide-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    799       Histidine biosynthesis trifunctional
FT                                protein.
FT                                /FTId=PRO_0000135913.
FT   REGION        1    229       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      230    312       Phosphoribosyl-ATP pyrophosphohydrolase.
FT   REGION      313    799       Histidinol dehydrogenase.
FT   ACT_SITE    687    687       By similarity.
FT   ACT_SITE    688    688       By similarity.
FT   METAL       618    618       Zinc (By similarity).
FT   METAL       621    621       Zinc (By similarity).
FT   METAL       721    721       Zinc (By similarity).
FT   METAL       780    780       Zinc (By similarity).
SQ   SEQUENCE   799 AA;  87734 MW;  35793E26EDB81B6B CRC64;
     MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP LVALSLPNAK
     FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR IVVEGNGVFH NQFLVNQKFS
     QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG LFTTLVVDQY ERCLGLVYSS KESIAKAIDL
     GRGVYYSRSR NEIWVKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE
     FKHGLVGLES LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA
     DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE EAPTGPIHLH
     VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD SALLEYTEKF DGVKLSTPVL
     NAPFPEEYFE GLTEEMKDAL DLSIENVRKF HAAQLPKETL EVETQPGVLC SRFPRPIEKV
     GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV
     LAGGAQAVAA MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV
     IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA MQLPRVDIVR
     KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG
     DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH
     RNAVKIRMSK LGLIPKDFQ
//