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UniProtKB/Swiss-Prot entry P00815


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

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Entry information
Entry name HIS2_YEAST
Primary accession number P00815
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on March 29, 2004 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 88)
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: HIS4
OrderedLocusNames: YCL030C
ORFNames: YCL30C, YCL183
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1016/0378-1119(82)90055-5; PubMed=7049842 [NCBI, ExPASy, EBI, Israel, Japan]
Donahue T.F., Farabaugh P.J., Fink G.R.;
"The nucleotide sequence of the HIS4 region of yeast.";
Gene 18:47-59(1982).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=1897318 [NCBI, ExPASy, EBI, Israel, Japan]
Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
"The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames.";
Yeast 7:533-538(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/357038a0; PubMed=1574125 [NCBI, ExPASy, EBI, Israel, Japan]
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[4]
SEQUENCE REVISION TO 375.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE OF 1-20.
DOI=10.1038/286352a0; PubMed=6250062 [NCBI, ExPASy, EBI, Israel, Japan]
Farabaugh P.J., Fink G.R.;
"Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair duplication.";
Nature 286:352-356(1980).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=2991923 [NCBI, ExPASy, EBI, Israel, Japan]
Roeder G.S., Rose A.B., Pearlman R.E.;
"Transposable element sequences involved in the enhancement of yeast gene expression.";
Proc. Natl. Acad. Sci. U.S.A. 82:5428-5432(1985).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
V01310; CAA24617.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59720; CAA42355.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01309; CAA24616.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11491; AAA67504.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11492; AAA67505.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11694; AAA18400.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11695; AAA18401.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11696; AAA18402.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17473; SHBY.
RefSeq NP_009900.2; -.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase P00815.
Protein-protein interaction databases
DIP DIP:6402N; -.
Organism-specific databases
CYGD YCL030c; -.
SGD S000000535; HIS4.
Yeast-GFP YCL030C.
Gene expression databases
ArrayExpress P00815; -.
GermOnline YCL030C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005622; Cellular component: intracellular (traceable author statement from SGD).
GO:0004399; Molecular function: histidinol dehydrogenase activity (traceable author statement from SGD).
GO:0004635; Molecular function: phosphoribosyl-AMP cyclohydrolase activity (traceable author statement from SGD).
GO:0004636; Molecular function: phosphoribosyl-ATP diphosphatase activity (traceable author statement from SGD).
GO:0000105; Biological process: histidine biosynthetic process (traceable author statement from SGD).
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.
BLOCKS P00815.
ProtoNet P00815.
Proteomic databases
PeptideAtlas P00815; -.
Genome annotation databases
Ensembl YCL030C; Saccharomyces cerevisiae. [Contig view]
GeneID 850327; -.
GenomeReviews X59720_GR; YCL030C.
KEGG sce:YCL030C; -.
NMPDR fig|4932.3.peg.620; -.
Phylogenomic databases
HOGENOM P00815; -.
Other
LinkHub P00815; -.
NextBio 965751; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Metal-binding; Multifunctional enzyme; NAD; Oxidoreductase; Phosphoprotein; 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_0000135914
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). 
MOD_RES   265   265        Phosphothreonine. 
CONFLICT   53    53        A -> R (in Ref. 1; CAA24617). 
CONFLICT   386   386        H -> Y (in Ref. 1; CAA24617). 
CONFLICT   402   403        AL -> VF (in Ref. 1; CAA24617). 
CONFLICT   441   441        D -> N (in Ref. 1; CAA24617). 
CONFLICT   794   794        I -> F (in Ref. 1; CAA24617). 
Sequence information
Length: 799 AA [This is the length of the unprocessed precursor] Molecular weight: 87721 Da [This is the MW of the unprocessed precursor] CRC64: 0B82D289BEAB754D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP LVALSLPSGK 

        70         80         90        100        110        120 
FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER VVVEENGVFS NQFMVKQKFS 

       130        140        150        160        170        180 
QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL 

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

       250        260        270        280        290        300 
FKHGLVGLES LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA 

       310        320        330        340        350        360 
DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE EKLTGPIHLD 

       370        380        390        400        410        420 
VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN SALLEYTEKF DGVKLSNPVL 

       430        440        450        460        470        480 
NAPFPEEYFE GLTEEMKEAL DLSIENVRKF HAAQLPTETL EVETQPGVLC SRFPRPIEKV 

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

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

       610        620        630        640        650        660 
IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA LQLPRVDIVR 

       670        680        690        700        710        720 
KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 

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

       790 
RNAVKIRMSK LGLIPKDFQ 

P00815 in FASTA format

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