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UniProtKB/Swiss-Prot entry Q12670

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HIS2_SACBA
Primary accession number Q12670
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Histidine biosynthesis trifunctional protein
Synonyms None
Includes Phosphoribosyl-AMP cyclohydrolase
     (EC 3.5.4.19)
Phosphoribosyl-ATP pyrophosphohydrolase
     (EC 3.6.1.31)
Histidinol dehydrogenase
     (HDH)
     (EC 1.1.1.23)
Gene name
Name: HIS2
From
Saccharomyces bayanus (Yeast) (Saccharomyces uvarum) [TaxID: 4931] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Carlsbergensis;
Porter G.L.;
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U13062; AAA21153.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S53349; S53349.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase Q12670.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0004635; Molecular function: phosphoribosyl-AMP cyclohydrolase activity (inferred from electronic annotation from InterPro).
GO:0004636; Molecular function: phosphoribosyl-ATP diphosphatase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016298; Histidine_synth_trifunct.
IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
IPR002496; PRA_CycOHase.
IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
PF01502; PRA-CH; 1.
PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001257; His_trifunctional; 1.
PRINTS PR00083; HOLDHDRGNASE.
ProDom PD002680; Histidinol_dh; 1.
PD002610; PRA_cyclohydro; 1.
PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
TIGR03188; histidine_hisI; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
Other
ProtoNet Q12670.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Metal-binding; Multifunctional enzyme; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   799  799     Histidine biosynthesis trifunctional protein. PRO_0000135913
REGION   1   229  229     Phosphoribosyl-AMP cyclohydrolase. 
REGION   230   312  83     Phosphoribosyl-ATP pyrophosphohydrolase. 
REGION   313   799  487     Histidinol dehydrogenase. 
ACT_SITE   687   687        By similarity. 
ACT_SITE   688   688        By similarity. 
METAL   618   618        Zinc (By similarity). 
METAL   621   621        Zinc (By similarity). 
METAL   721   721        Zinc (By similarity). 
METAL   780   780        Zinc (By similarity). 
Sequence information
Length: 799 AA [This is the length of the unprocessed precursor] Molecular weight: 87734 Da [This is the MW of the unprocessed precursor] CRC64: 35793E26EDB81B6B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP LVALSLPNAK 

        70         80         90        100        110        120 
FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR IVVEGNGVFH NQFLVNQKFS 

       130        140        150        160        170        180 
QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG LFTTLVVDQY ERCLGLVYSS KESIAKAIDL 

       190        200        210        220        230        240 
GRGVYYSRSR NEIWVKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE 

       250        260        270        280        290        300 
FKHGLVGLES LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA 

       310        320        330        340        350        360 
DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE EAPTGPIHLH 

       370        380        390        400        410        420 
VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD SALLEYTEKF DGVKLSTPVL 

       430        440        450        460        470        480 
NAPFPEEYFE GLTEEMKDAL DLSIENVRKF HAAQLPKETL EVETQPGVLC SRFPRPIEKV 

       490        500        510        520        530        540 
GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV 

       550        560        570        580        590        600 
LAGGAQAVAA MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 

       610        620        630        640        650        660 
IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA MQLPRVDIVR 

       670        680        690        700        710        720 
KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 

       730        740        750        760        770        780 
DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH 

       790 
RNAVKIRMSK LGLIPKDFQ
Q12670 in FASTA format

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