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Q27685 (PGKC_LEIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase, glycosomal

Short name=Phosphoglycerate kinase C
EC=2.7.2.3
Gene names
Name:PGKC
OrganismLeishmania mexicana
Taxonomic identifier5665 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00145

Subcellular location

Glycosome HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentGlycosome
Peroxisome
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentglycosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Phosphoglycerate kinase, glycosomal HAMAP-Rule MF_00145
PRO_0000145856

Regions

Nucleotide binding372 – 3754ATP By similarity
Region24 – 263Substrate binding By similarity
Region62 – 654Substrate binding By similarity

Sites

Binding site391Substrate By similarity
Binding site1321Substrate By similarity
Binding site1691Substrate By similarity
Binding site2201ATP By similarity
Binding site3421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27685 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 03C3B8B12DF7DAB4

FASTA47951,499
        10         20         30         40         50         60 
MSLVLKKSID DVALKDKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM 

        70         80         90        100        110        120 
SHLGRPKGAR MSDPKPEKGV RGYEEAATLR PVAAALSELL EKKVAFAPDC LNASIYVSKL 

       130        140        150        160        170        180 
KRGDVLLLEN VRFYTEEGSK KEEEADAMAK VLASYADLYV SDAFGTAHRD SATMTGIPKV 

       190        200        210        220        230        240 
LGSGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IELLDNMLGR INYLVIGGAM 

       250        260        270        280        290        300 
AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERGVQVL LPVDHVCNKE FKAVDSPLVT 

       310        320        330        340        350        360 
EDVDVPDGYM ALDIGPKTIH MYEEVIGRCK SAIWNGPMGV FEMPCYSKGT FAVAKAMGTG 

       370        380        390        400        410        420 
TQKDGLLSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE LLEGKTLPGV AILTDKEVKG 

       430        440        450        460        470 
RGPLLKCACG GASPSNESCP RRREGIWGGG FIVTEIVKLV GALLIGIFIG RRLNTKLIR 

« Hide

References

[1]"Organization, sequence and stage-specific expression of the phosphoglycerate kinase genes of Leishmania mexicana mexicana."
Adje C.A., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 90:155-168(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MHOM/BZ/84/BEL46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98487 Genomic DNA. Translation: CAA67113.1.

3D structure databases

ProteinModelPortalQ27685.
SMRQ27685. Positions 6-416.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00185.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGKC_LEIME
AccessionPrimary (citable) accession number: Q27685
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways