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B0B8R9 (PGK_CHLT2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase
EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:CTL0062
OrganismChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP]
Taxonomic identifier471472 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia ›

Protein attributes

Sequence length403 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.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Sequence caution

The sequence AAB41227.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096327

Regions

Nucleotide binding357 – 3604ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1541Substrate By similarity
Binding site2071ATP By similarity
Binding site2991ATP; via carbonyl oxygen By similarity
Binding site3301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0B8R9 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 4E477DCF67091C79

FASTA40343,071
        10         20         30         40         50         60 
MDKLSIRDLS LEGKKVLVRV DFNVPIKDGK ILDDVRIRSA MPTIHYLLKQ DAAVILVSHL 

        70         80         90        100        110        120 
GRPKGGVFEE AYSLAPIVPV LEGYLGHHVP LSPDCIGEVA RQAVAQLSPG RVLLLENVRF 

       130        140        150        160        170        180 
HKGEEHPDED PSFAIELAAY ADFYVNDAFG TSHRKHASVY RVPQLFPDRA AAGFLMEKEL 

       190        200        210        220        230        240 
EFLGQHLLVE PKRPFTAILG GAKMSSKIGV IEALLSCVDH LVLAGGMGYT FLRAMNRQVG 

       250        260        270        280        290        300 
NSLVEESGIP LAKKVLEKAQ ALGVKIHLPV DAKVAKQCDS GEDWRELSIQ EGIPEGLAGF 

       310        320        330        340        350        360 
DIGAQTIELF SKVIQESATI FWNGPVGVYE VPPFDQGSKA IAQCLASHSS AVTVVGGGDA 

       370        380        390        400 
AAVVALAGCT SQISHVSTGG GASLEFLEKG SLPGTEILSP AQS

« Hide

References

« Hide 'large scale' references
[1]"Glucose metabolism in Chlamydia trachomatis: the 'energy parasite' hypothesis revisited."
Iliffe-Lee E.R., McClarty G.
Mol. Microbiol. 33:177-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 434/Bu / ATCC VR-902B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U83197 Genomic DNA. Translation: AAB41227.1. Different initiation.
AM884176 Genomic DNA. Translation: CAP03506.1.
RefSeqYP_001654153.1. NC_010287.1.

3D structure databases

ProteinModelPortalB0B8R9.
ModBaseSearch...

Protein-protein interaction databases

STRING471472.CTL0062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP03506; CAP03506; CTL0062.
GeneID5858720.
KEGGctb:CTL0062.
PATRIC20375556. VBIChlTra32542_0067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAKFGLADK.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycCTRA471472:GJ9M-68-MONOMER.
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. PGK. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_CHLT2
AccessionPrimary (citable) accession number: B0B8R9
Secondary accession number(s): O84699, P94686
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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