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P00815 (HIS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine biosynthesis trifunctional protein

Including the following 3 domains:

  1. Phosphoribosyl-AMP cyclohydrolase
    EC=3.5.4.19
  2. Phosphoribosyl-ATP pyrophosphohydrolase
    EC=3.6.1.31
  3. Histidinol dehydrogenase
    Short name=HDH
    EC=1.1.1.23
Gene names
Name:HIS4
Ordered Locus Names:YCL030C
ORF Names:YCL183, YCL30C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP-Rule MF_01024

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate. HAMAP-Rule MF_01024

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP-Rule MF_01024

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.

Sequence similarities

In the C-terminal section; belongs to the histidinol dehydrogenase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FMP48P532332EBI-8334,EBI-9664

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 799799Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135914

Regions

Region1 – 229229Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region230 – 31283Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region313 – 799487Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site6871 By similarity
Active site6881 By similarity
Metal binding6181Zinc By similarity
Metal binding6211Zinc By similarity
Metal binding7211Zinc By similarity
Metal binding7801Zinc By similarity

Experimental info

Sequence conflict531A → R in CAA24617. Ref.1
Sequence conflict3861H → Y in CAA24617. Ref.1
Sequence conflict402 – 4032AL → VF in CAA24617. Ref.1
Sequence conflict4411D → N in CAA24617. Ref.1
Sequence conflict7941I → F in CAA24617. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00815 [UniParc].

Last modified March 29, 2004. Version 3.
Checksum: 0B82D289BEAB754D

FASTA79987,721
        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 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the HIS4 region of yeast."
Donahue T.F., Farabaugh P.J., Fink G.R.
Gene 18:47-59(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames."
Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.
Yeast 7:533-538(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The complete DNA sequence of yeast chromosome III."
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. expand/collapse author list , 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.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 375.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair duplication."
Farabaugh P.J., Fink G.R.
Nature 286:352-356(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
[7]"Transposable element sequences involved in the enhancement of yeast gene expression."
Roeder G.S., Rose A.B., Pearlman R.E.
Proc. Natl. Acad. Sci. U.S.A. 82:5428-5432(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01310 Genomic DNA. Translation: CAA24617.1.
X59720 Genomic DNA. Translation: CAA42355.2.
V01309 Genomic DNA. Translation: CAA24616.1.
M11491 Genomic DNA. Translation: AAA67504.1.
M11492 Genomic DNA. Translation: AAA67505.1.
M11694 Unassigned DNA. Translation: AAA18400.1.
M11695 Unassigned DNA. Translation: AAA18401.1.
M11696 Unassigned DNA. Translation: AAA18402.1.
BK006937 Genomic DNA. Translation: DAA07454.1.
PIRSHBY. S17473.
RefSeqNP_009900.2. NM_001178675.1.

3D structure databases

ProteinModelPortalP00815.
SMRP00815. Positions 164-238, 247-324, 371-791.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30953. 25 interactions.
DIPDIP-6402N.
IntActP00815. 14 interactions.
MINTMINT-617364.
STRING4932.YCL030C.

Proteomic databases

PaxDbP00815.
PeptideAtlasP00815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL030C; YCL030C; YCL030C.
GeneID850327.
KEGGsce:YCL030C.

Organism-specific databases

CYGDYCL030c.
SGDS000000535. HIS4.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK14152.
OMANIRKFHA.
OrthoDBEOG7DJSVM.

Enzyme and pathway databases

BioCycYEAST:YCL030C-MONOMER.
UniPathwayUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Gene expression databases

GenevestigatorP00815.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFPIRSF001257. His_trifunctional. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965751.

Entry information

Entry nameHIS2_YEAST
AccessionPrimary (citable) accession number: P00815
Secondary accession number(s): D6VQY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2004
Last modified: March 19, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways