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P00815

- HIS2_YEAST

UniProt

P00815 - HIS2_YEAST

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Protein
Histidine biosynthesis trifunctional protein
Gene
HIS4, YCL030C, YCL183, YCL30C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.UniRule annotation
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.UniRule annotation
L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Binds 1 zinc ion By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi618 – 6181Zinc By similarity
Metal bindingi621 – 6211Zinc By similarity
Active sitei687 – 6871 By similarity
Active sitei688 – 6881 By similarity
Metal bindingi721 – 7211Zinc By similarity
Metal bindingi780 – 7801Zinc By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. NAD binding Source: InterPro
  3. histidinol dehydrogenase activity Source: SGD
  4. phosphoribosyl-AMP cyclohydrolase activity Source: SGD
  5. phosphoribosyl-ATP diphosphatase activity Source: SGD
  6. protein binding Source: IntAct
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. histidine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YCL030C-MONOMER.
UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine biosynthesis trifunctional protein
Including the following 3 domains:
Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
Phosphoribosyl-ATP pyrophosphohydrolase (EC:3.6.1.31)
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:HIS4
Ordered Locus Names:YCL030C
ORF Names:YCL183, YCL30C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCL030c.
SGDiS000000535. HIS4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 799799Histidine biosynthesis trifunctional proteinUniRule annotation
PRO_0000135914Add
BLAST

Proteomic databases

MaxQBiP00815.
PaxDbiP00815.
PeptideAtlasiP00815.

Expressioni

Gene expression databases

GenevestigatoriP00815.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FMP48P532332EBI-8334,EBI-9664

Protein-protein interaction databases

BioGridi30953. 25 interactions.
DIPiDIP-6402N.
IntActiP00815. 14 interactions.
MINTiMINT-617364.
STRINGi4932.YCL030C.

Structurei

3D structure databases

ProteinModelPortaliP00815.
SMRiP00815. Positions 164-238, 356-791.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229Phosphoribosyl-AMP cyclohydrolaseUniRule annotation
Add
BLAST
Regioni230 – 31283Phosphoribosyl-ATP pyrophosphohydrolaseUniRule annotation
Add
BLAST
Regioni313 – 799487Histidinol dehydrogenaseUniRule annotation
Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK14152.
OMAiNIRKFHA.
OrthoDBiEOG7DJSVM.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. 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]
PfamiPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFiPIRSF001257. His_trifunctional. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00815-1 [UniParc]FASTAAdd to Basket

« Hide

MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP    50
LVALSLPSGK FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER 100
VVVEENGVFS NQFMVKQKFS QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG 150
LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL GRGVYYSRSR NEIWIKGETS 200
GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE FKHGLVGLES 250
LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA 300
DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE 350
EKLTGPIHLD VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN 400
SALLEYTEKF DGVKLSNPVL NAPFPEEYFE GLTEEMKEAL DLSIENVRKF 450
HAAQLPTETL EVETQPGVLC SRFPRPIEKV GLYIPGGTAI LPSTALMLGV 500
PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGASKIV LAGGAQAVAA 550
MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 600
IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA 650
LQLPRVDIVR KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV 700
KLVDNAGSVF VGAYTPESCG DYSSGTNHTL PTYGYARQYS GANTATFQKF 750
ITAQNITPEG LENIGRAVMC VAKKEGLDGH RNAVKIRMSK LGLIPKDFQ 799
Length:799
Mass (Da):87,721
Last modified:March 29, 2004 - v3
Checksum:i0B82D289BEAB754D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531A → R in CAA24617. 1 Publication
Sequence conflicti386 – 3861H → Y in CAA24617. 1 Publication
Sequence conflicti402 – 4032AL → VF in CAA24617. 1 Publication
Sequence conflicti441 – 4411D → N in CAA24617. 1 Publication
Sequence conflicti794 – 7941I → F in CAA24617. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS17473. SHBY.
RefSeqiNP_009900.2. NM_001178675.1.

Genome annotation databases

EnsemblFungiiYCL030C; YCL030C; YCL030C.
GeneIDi850327.
KEGGisce:YCL030C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S17473. SHBY.
RefSeqi NP_009900.2. NM_001178675.1.

3D structure databases

ProteinModelPortali P00815.
SMRi P00815. Positions 164-238, 356-791.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30953. 25 interactions.
DIPi DIP-6402N.
IntActi P00815. 14 interactions.
MINTi MINT-617364.
STRINGi 4932.YCL030C.

Proteomic databases

MaxQBi P00815.
PaxDbi P00815.
PeptideAtlasi P00815.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCL030C ; YCL030C ; YCL030C .
GeneIDi 850327.
KEGGi sce:YCL030C.

Organism-specific databases

CYGDi YCL030c.
SGDi S000000535. HIS4.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K14152.
OMAi NIRKFHA.
OrthoDBi EOG7DJSVM.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00007 .
UPA00031 ; UER00008 .
UPA00031 ; UER00014 .
BioCyci YEAST:YCL030C-MONOMER.

Miscellaneous databases

NextBioi 965751.

Gene expression databases

Genevestigatori P00815.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. 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 ]
Pfami PF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view ]
PIRSFi PIRSF001257. His_trifunctional. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
ProDomi PD002610. PRA_CycHdrlase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHIS2_YEAST
AccessioniPrimary (citable) accession number: P00815
Secondary accession number(s): D6VQY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2004
Last modified: June 11, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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