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O62619

- KPYK_DROME

UniProt

O62619 - KPYK_DROME

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Protein

Pyruvate kinase

Gene

PyK

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateBy similarity
Metal bindingi78 – 781PotassiumBy similarity
Metal bindingi80 – 801PotassiumBy similarity
Metal bindingi116 – 1161PotassiumBy similarity
Metal bindingi117 – 1171Potassium; via carbonyl oxygenBy similarity
Sitei273 – 2731Transition state stabilizerBy similarity
Metal bindingi275 – 2751MagnesiumBy similarity
Binding sitei298 – 2981Substrate; via amide nitrogenBy similarity
Metal bindingi299 – 2991MagnesiumBy similarity
Binding sitei299 – 2991Substrate; via amide nitrogenBy similarity
Binding sitei331 – 3311SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

ReactomeiREACT_206319. Glycolysis.
REACT_213793. ChREBP activates metabolic gene expression.
REACT_251274. Regulation of gene expression in beta cells.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:PyK
ORF Names:CG7070
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0267385. PyK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Pyruvate kinasePRO_0000112099Add
BLAST

Proteomic databases

PaxDbiO62619.
PRIDEiO62619.

Expressioni

Tissue specificityi

In adults expressed predominantly in the thorax.1 Publication

Developmental stagei

Low levels in larvae and pupae, but increases in young adults, becoming relatively stable in two-day-old flies.1 Publication

Gene expression databases

BgeeiO62619.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi67578. 14 interactions.
DIPiDIP-19290N.
IntActiO62619. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliO62619.
SMRiO62619. Positions 30-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
InParanoidiO62619.
KOiK00873.
OMAiFIPANSE.
OrthoDBiEOG78M01Q.
PhylomeDBiO62619.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: O62619-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVNVTIYDEA PQLKPNEVPQ NMAAGADTQL EHMCRLQFDS PVPHVRLSGI
60 70 80 90 100
VCTIGPASSS VEMLEKMMAT GMNIARMNFS HGSHEYHAAT VANVRQAVKN
110 120 130 140 150
YSAKLGYEHP VAIALDTKGP EIRTGLIGGS GTAEIELKKG EKIKLTTNKE
160 170 180 190 200
FLEKGSLEIV YVDYENIVNV VKPGNRVFVD DGLISLIVRE VGKDSLTCEV
210 220 230 240 250
ENGGSLGSRK GVNLPGVPVD LPAVSEKDKS DLLFGVEQEV DMIFASFIRN
260 270 280 290 300
AAALTEIRKV LGEKGKNIKI ISKIENQQGM HNLDEIIEAG DGIMVARGDL
310 320 330 340 350
GIEIPAEKVF LAQKAMIARC NKAGKPVICA TQMLESMVKK PRPTRAEISD
360 370 380 390 400
VANAVLDGAD CVMLSGETAK GEYPLECVLT MAKTCKEAEA ALWHQNLFND
410 420 430 440 450
LVRGAGTIDA SHAAAIAAVE AATKAKASAI VVITTSGKSA FQVSKYRPRC
460 470 480 490 500
PIIAVTRFAQ TARQAHLYRG LVPLIYKEPG LGDWLKDVDV RVQFGLQVGK
510 520 530
KNGFIKTGDS VVVVTGWKQG SGFTNTIRIV TVE
Length:533
Mass (Da):57,440
Last modified:January 27, 2003 - v2
Checksum:iA8376B72F040EEDB
GO
Isoform B (identifier: O62619-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: No experimental confirmation available.

Show »
Length:512
Mass (Da):55,059
Checksum:i4ED4A31F0686874B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801D → N in AAC16244. 1 PublicationCurated
Sequence conflicti180 – 1801D → N in AAC15808. 1 PublicationCurated
Sequence conflicti271 – 2711I → F in AAO24935. (PubMed:12537569)Curated
Sequence conflicti397 – 3971L → F in AAC16244. 1 PublicationCurated
Sequence conflicti397 – 3971L → F in AAC15808. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform B. 1 PublicationVSP_002885Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062478 Genomic DNA. Translation: AAC16244.1.
AF061507 mRNA. Translation: AAC15808.1.
AE014297 Genomic DNA. Translation: AAF55979.3.
AE014297 Genomic DNA. Translation: AAN14373.1.
AY118442 mRNA. Translation: AAM48471.1.
BT003180 mRNA. Translation: AAO24935.1.
BT082045 mRNA. Translation: ACO95723.1.
RefSeqiNP_524448.3. NM_079724.3. [O62619-1]
NP_732723.1. NM_170004.2. [O62619-2]
UniGeneiDm.7108.

Genome annotation databases

EnsemblMetazoaiFBtr0084214; FBpp0083611; FBgn0003178. [O62619-1]
GeneIDi42620.
KEGGidme:Dmel_CG7070.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062478 Genomic DNA. Translation: AAC16244.1 .
AF061507 mRNA. Translation: AAC15808.1 .
AE014297 Genomic DNA. Translation: AAF55979.3 .
AE014297 Genomic DNA. Translation: AAN14373.1 .
AY118442 mRNA. Translation: AAM48471.1 .
BT003180 mRNA. Translation: AAO24935.1 .
BT082045 mRNA. Translation: ACO95723.1 .
RefSeqi NP_524448.3. NM_079724.3. [O62619-1 ]
NP_732723.1. NM_170004.2. [O62619-2 ]
UniGenei Dm.7108.

3D structure databases

ProteinModelPortali O62619.
SMRi O62619. Positions 30-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67578. 14 interactions.
DIPi DIP-19290N.
IntActi O62619. 3 interactions.

Proteomic databases

PaxDbi O62619.
PRIDEi O62619.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0084214 ; FBpp0083611 ; FBgn0003178 . [O62619-1 ]
GeneIDi 42620.
KEGGi dme:Dmel_CG7070.

Organism-specific databases

CTDi 42620.
FlyBasei FBgn0267385. PyK.

Phylogenomic databases

eggNOGi COG0469.
GeneTreei ENSGT00390000008859.
InParanoidi O62619.
KOi K00873.
OMAi FIPANSE.
OrthoDBi EOG78M01Q.
PhylomeDBi O62619.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
Reactomei REACT_206319. Glycolysis.
REACT_213793. ChREBP activates metabolic gene expression.
REACT_251274. Regulation of gene expression in beta cells.

Miscellaneous databases

ChiTaRSi PyK. fly.
GenomeRNAii 42620.
NextBioi 829729.
PROi O62619.

Gene expression databases

Bgeei O62619.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA cloning and analysis of gene structure of pyruvate kinase from Drosophila melanogaster."
    Chien Y.-C., Zhu Y.-J., Chuen C.-M.
    Zool. Stud. 38:322-332(1999)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
    Strain: Canton-S.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
    Strain: Berkeley.
    Tissue: Embryo and Head.
  5. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
  6. "Localization of a dosage sensitive region for pyruvate kinase in Drosophila melanogaster."
    Rust K.J., Collier G.E.
    J. Hered. 76:39-44(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiKPYK_DROME
AccessioniPrimary (citable) accession number: O62619
Secondary accession number(s): C3KGI0
, Q86PE3, Q8MT14, Q9VD24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 27, 2003
Last modified: November 26, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3