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P00560

- PGK_YEAST

UniProt

P00560 - PGK_YEAST

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Protein

Phosphoglycerate kinase

Gene

PGK1

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

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Substrate2 Publications
Binding sitei122 – 1221Substrate2 Publications
Binding sitei169 – 1691Substrate2 Publications
Binding sitei218 – 2181ATP
Binding sitei311 – 3111ATP; via carbonyl oxygen
Binding sitei335 – 3351ATP
Binding sitei342 – 3421ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi371 – 3744ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate kinase activity Source: SGD

GO - Biological processi

  1. gluconeogenesis Source: SGD
  2. glycolytic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YCR012W-MONOMER.
ReactomeiREACT_229625. Glycolysis.
REACT_235985. Gluconeogenesis.
SABIO-RKP00560.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
Gene namesi
Name:PGK1
Ordered Locus Names:YCR012W
ORF Names:YCR12W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

SGDiS000000605. PGK1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221R → K: 2-fold reduction of Vmax. 1 Publication
Mutagenesisi22 – 221R → M: 7-fold reduction of Vmax. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 416415Phosphoglycerate kinasePRO_0000145893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei93 – 931Phosphothreonine1 Publication
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei154 – 1541Phosphoserine1 Publication
Modified residuei172 – 1721Phosphoserine1 Publication
Modified residuei203 – 2031Phosphothreonine1 Publication
Modified residuei241 – 2411Phosphothreonine1 Publication
Modified residuei298 – 2981Phosphothreonine1 Publication
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei331 – 3311Phosphothreonine3 Publications
Modified residuei392 – 3921Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00560.
PaxDbiP00560.
PeptideAtlasiP00560.
PRIDEiP00560.

2D gel databases

COMPLUYEAST-2DPAGEP00560.

Expressioni

Gene expression databases

GenevestigatoriP00560.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi30991. 84 interactions.
DIPiDIP-4152N.
IntActiP00560. 45 interactions.
MINTiMINT-484961.
STRINGi4932.YCR012W.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi18 – 225Combined sources
Beta strandi29 – 357Combined sources
Helixi38 – 5114Combined sources
Beta strandi56 – 616Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 753Combined sources
Helixi78 – 8811Combined sources
Beta strandi92 – 943Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 1088Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi114 – 1174Combined sources
Helixi121 – 1233Combined sources
Turni125 – 1284Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi136 – 1394Combined sources
Helixi142 – 15312Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 1663Combined sources
Helixi172 – 1754Combined sources
Beta strandi182 – 1843Combined sources
Helixi186 – 20015Combined sources
Beta strandi204 – 2118Combined sources
Turni216 – 2183Combined sources
Helixi219 – 2268Combined sources
Beta strandi230 – 2356Combined sources
Helixi236 – 2383Combined sources
Helixi239 – 2468Combined sources
Helixi247 – 2526Combined sources
Helixi258 – 27316Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi282 – 29110Combined sources
Beta strandi296 – 3005Combined sources
Turni301 – 3033Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi310 – 3145Combined sources
Helixi316 – 32813Combined sources
Beta strandi330 – 3367Combined sources
Helixi344 – 3463Combined sources
Helixi348 – 36215Combined sources
Beta strandi366 – 3694Combined sources
Helixi373 – 3808Combined sources
Helixi384 – 3863Combined sources
Beta strandi387 – 3904Combined sources
Helixi395 – 4017Combined sources
Helixi407 – 4104Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FW8X-ray2.30A74-416[»]
1QPGX-ray2.40A2-416[»]
3PGKX-ray2.50A2-416[»]
ProteinModelPortaliP00560.
SMRiP00560. Positions 2-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00560.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 263Substrate binding
Regioni63 – 664Substrate binding

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
InParanoidiP00560.
KOiK00927.
OMAiFPVDYVT.
OrthoDBiEOG71K6D7.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00560-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLSSKLSVQ DLDLKDKRVF IRVDFNVPLD GKKITSNQRI VAALPTIKYV
60 70 80 90 100
LEHHPRYVVL ASHLGRPNGE RNEKYSLAPV AKELQSLLGK DVTFLNDCVG
110 120 130 140 150
PEVEAAVKAS APGSVILLEN LRYHIEEEGS RKVDGQKVKA SKEDVQKFRH
160 170 180 190 200
ELSSLADVYI NDAFGTAHRA HSSMVGFDLP QRAAGFLLEK ELKYFGKALE
210 220 230 240 250
NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIIIGGGMAF TFKKVLENTE
260 270 280 290 300
IGDSIFDKAG AEIVPKLMEK AKAKGVEVVL PVDFIIADAF SADANTKTVT
310 320 330 340 350
DKEGIPAGWQ GLDNGPESRK LFAATVAKAK TIVWNGPPGV FEFEKFAAGT
360 370 380 390 400
KALLDEVVKS SAAGNTVIIG GGDTATVAKK YGVTDKISHV STGGGASLEL
410
LEGKELPGVA FLSEKK
Length:416
Mass (Da):44,738
Last modified:January 23, 2007 - v2
Checksum:i378AB944DB34EFF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851G → S AA sequence (PubMed:7287307)Curated
Sequence conflicti191 – 1911E → I AA sequence (PubMed:7287307)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01342 Genomic DNA. Translation: AAA88729.1.
X59720 Genomic DNA. Translation: CAA42329.2.
M14438 Genomic DNA. Translation: AAA34864.1.
K00553 Genomic DNA. Translation: AAA34863.1. Sequence problems.
BK006937 Genomic DNA. Translation: DAA07490.1.
PIRiS19422. KIBYG.
RefSeqiNP_009938.2. NM_001178725.1.

Genome annotation databases

EnsemblFungiiYCR012W; YCR012W; YCR012W.
GeneIDi850370.
KEGGisce:YCR012W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01342 Genomic DNA. Translation: AAA88729.1 .
X59720 Genomic DNA. Translation: CAA42329.2 .
M14438 Genomic DNA. Translation: AAA34864.1 .
K00553 Genomic DNA. Translation: AAA34863.1 . Sequence problems.
BK006937 Genomic DNA. Translation: DAA07490.1 .
PIRi S19422. KIBYG.
RefSeqi NP_009938.2. NM_001178725.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FW8 X-ray 2.30 A 74-416 [» ]
1QPG X-ray 2.40 A 2-416 [» ]
3PGK X-ray 2.50 A 2-416 [» ]
ProteinModelPortali P00560.
SMRi P00560. Positions 2-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30991. 84 interactions.
DIPi DIP-4152N.
IntActi P00560. 45 interactions.
MINTi MINT-484961.
STRINGi 4932.YCR012W.

Chemistry

BindingDBi P00560.
ChEMBLi CHEMBL2674.

2D gel databases

COMPLUYEAST-2DPAGE P00560.

Proteomic databases

MaxQBi P00560.
PaxDbi P00560.
PeptideAtlasi P00560.
PRIDEi P00560.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCR012W ; YCR012W ; YCR012W .
GeneIDi 850370.
KEGGi sce:YCR012W.

Organism-specific databases

SGDi S000000605. PGK1.

Phylogenomic databases

eggNOGi COG0126.
GeneTreei ENSGT00390000008820.
HOGENOMi HOG000227107.
InParanoidi P00560.
KOi K00927.
OMAi FPVDYVT.
OrthoDBi EOG71K6D7.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00185 .
BioCyci YEAST:YCR012W-MONOMER.
Reactomei REACT_229625. Glycolysis.
REACT_235985. Gluconeogenesis.
SABIO-RK P00560.

Miscellaneous databases

EvolutionaryTracei P00560.
NextBioi 965861.
PROi P00560.

Gene expression databases

Genevestigatori P00560.

Family and domain databases

Gene3Di 3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPi MF_00145. Phosphoglyc_kinase.
InterProi IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view ]
PANTHERi PTHR11406. PTHR11406. 1 hit.
Pfami PF00162. PGK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000724. Pgk. 1 hit.
PRINTSi PR00477. PHGLYCKINASE.
SUPFAMi SSF53748. SSF53748. 1 hit.
PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of the Saccharomyces cerevisiae gene for 3-phosphoglycerate kinase."
    Hitzeman R.A., Hagie F.E., Hayflick J.S., Chen C.Y., Seeburg P.H., Derynck R.
    Nucleic Acids Res. 10:7791-7808(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm of chromosome III from Saccharomyces cerevisiae reveals seven open reading frames including the RVS161, ADP1 and PGK genes."
    Skala J., Purnelle B., Goffeau A.
    Yeast 8:409-417(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Structural studies on yeast 3-phosphoglycerate kinase. Linear arrangement of the CNBr fragments, partial amino acid sequence of the inner part of the polypeptide chain, and analyses of the N-terminal domain of the protein."
    Fattoum A., Roustan C., Karoui D., Feinberg J., Pradel L.-A., Gregoire J., Rochat H.
    Int. J. Pept. Protein Res. 17:393-400(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 173-202 AND 238-270.
  6. "The complete amino acid sequence of yeast phosphoglycerate kinase."
    Perkins R.E., Conroy S.C., Dunbar B., Fothergill L.A., Tuite M.F., Dobson M.J., Kingsman S.M., Kingsman A.J.
    Biochem. J. 211:199-218(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-416.
  7. Cited for: PRELIMINARY PROTEIN SEQUENCE OF 268-398, NUCLEOTIDE SEQUENCE OF 2-7.
  8. "Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins."
    Norbeck J., Blomberg A.
    Yeast 13:1519-1534(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 150-161; 198-209 AND 245-256.
    Strain: ATCC 44827 / SKQ2N.
  9. "Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21."
    Walker P.A., Joao H.C., Littlechild J.A., Wiliams R.J.P., Watson H.C.
    Eur. J. Biochem. 207:29-37(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-22.
  10. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-331 AND THR-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; THR-203; THR-241 AND THR-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-172; THR-298; SER-318; THR-331 AND THR-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Sequence and structure of yeast phosphoglycerate kinase."
    Watson H.C., Walker N.P.C., Shaw P.J., Bryant T.N., Wendell P.L., Fothergill L.A., Perkins R.E., Conroy S.C., Dobson M.J., Tuite M.F., Kingsman A.J., Kingsman S.M.
    EMBO J. 1:1635-1640(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG.
  20. "Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate."
    McPhillips T.M., Hsu B.T., Sherman M.A., Mas M.T., Rees D.C.
    Biochemistry 35:4118-4127(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLN-66 IN COMPLEX WITH SUBSTRATE AND ATP ANALOG.

Entry informationi

Entry nameiPGK_YEAST
AccessioniPrimary (citable) accession number: P00560
Secondary accession number(s): D6VR21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 314000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3