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Protein

Phosphoglycerate kinase, glycosomal

Gene

PGKC

Organism
Crithidia fasciculata
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391SubstrateBy similarity
Binding sitei132 – 1321SubstrateBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Binding sitei220 – 2201ATPBy similarity
Binding sitei342 – 3421ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi372 – 3754ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate 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, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase, glycosomal (EC:2.7.2.3)
Short name:
Phosphoglycerate kinase C
Gene namesi
Name:PGKC
Synonyms:PGK-C
OrganismiCrithidia fasciculata
Taxonomic identifieri5656 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Subcellular locationi

GO - Cellular componenti

  1. glycosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Phosphoglycerate kinase, glycosomalPRO_0000145850Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP08967.
SMRiP08967. Positions 6-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 263Substrate bindingBy similarity
Regioni62 – 654Substrate bindingBy similarity
Regioni417 – 45539Topogenic signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi422 – 4276Poly-Ala

Domaini

This glycosomal PGK has a C-terminal extension of 38 AA which is not present in the cytosolic isoenzyme. This domain most likely serves as topogenic signal to direct the glycosomal PKG to the glycosome.

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR027250. Pgk_euglenozoa.
IPR001576. 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.
PIRSF500126. Pgk_euglenozoa. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVPKKSID DAVVKGKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV
60 70 80 90 100
LKEGGSCILM SHLGRPKGAK MSDPKPAKSV RGYEEAATLR PVAARLSELL
110 120 130 140 150
GQKVEFAPDC LDAASYAAKL KGGDVLLLEN VRFYAEEGSK KEEERDAMAK
160 170 180 190 200
VLAAYGDVYV SDAFGTAHRD SADMTGIPKV LGAGYAGYLM EKEINYFAQV
210 220 230 240 250
LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM AYTFQKAQGH
260 270 280 290 300
AIGISMCEED KLDLAKSLLK KAQERNVEVL LPVDHVCNKE FQGVDAPLVT
310 320 330 340 350
KDVEIPEGYM ALDIGPKTIK IYEDVIAKCK STIWNGPMGV FEMPCYSKGT
360 370 380 390 400
FAVAKAMGNG TQKNGLMSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE
410 420 430 440 450
LLEGKSLPGV TVLTNKDAKA PAAAAAAGGD CPCGSGCAAV PAAATATVSM

VLASP
Length:455
Mass (Da):47,843
Last modified:November 1, 1988 - v1
Checksum:iD8BF53AE5A0E1BFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07459 Genomic DNA. Translation: CAA30342.1.
PIRiS00487. TVCRGG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07459 Genomic DNA. Translation: CAA30342.1.
PIRiS00487. TVCRGG.

3D structure databases

ProteinModelPortaliP08967.
SMRiP08967. Positions 6-416.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR027250. Pgk_euglenozoa.
IPR001576. 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.
PIRSF500126. Pgk_euglenozoa. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase of Crithidia fasciculata resides in a carboxy-terminal extension."
    Swinkels B.W., Evers R., Borst P.
    EMBO J. 7:1159-1165(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPGKC_CRIFA
AccessioniPrimary (citable) accession number: P08967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: January 7, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.