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B0CD95 (PGK_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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

EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:AM1_0637
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

Protein attributes

Sequence length401 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

Cytoplasm Potential HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000076577

Regions

Nucleotide binding357 – 3604ATP By similarity
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity

Sites

Binding site401Substrate By similarity
Binding site1221Substrate By similarity
Binding site1551Substrate By similarity
Binding site2061ATP By similarity
Binding site2971ATP; via carbonyl oxygen By similarity
Binding site3281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CD95 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 7D414EB97EC3D54D

FASTA40141,862
        10         20         30         40         50         60 
MSKKTIANLT SADLSGKRVL VRADFNVPLD GDGKITDDTR IRAALPTIQD LTSKGAKVIL 

        70         80         90        100        110        120 
ASHFGRPKGQ VNESMRLTPV AARLSELLGQ AVTKCDDCIG DEVAAKVGAL QNGQVALLEN 

       130        140        150        160        170        180 
VRFHSGEEAN DPEFARQLAS VADLYVNDAF GTAHRAHAST EGVTHHLSPS VAGYLIEKEL 

       190        200        210        220        230        240 
KYLQAAIEGP QRPLAAIVGG SKVSSKIGVI ETLLDKVDKL LIGGGMIFTF YKARGLAVGK 

       250        260        270        280        290        300 
SLVEEDKLDL ARTLEAKAKE KGVALLLPSD VVVADNFAAD ANAQTVSINN IPDGWMGLDI 

       310        320        330        340        350        360 
GPNSVKEFQA ALSDCKTVIW NGPMGVFEFD KFAAGTDAVA HSLAAITETG ADTIIGGGDS 

       370        380        390        400 
VAAVEKVGVA EKMSHISTGG GASLELLEGK VLPGIAALDE A 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW25686.1.
RefSeqYP_001515000.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CD95.
SMRB0CD95. Positions 1-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_0637.

Proteomic databases

PRIDEB0CD95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW25686; ABW25686; AM1_0637.
GeneID5679465.
KEGGamr:AM1_0637.
PATRIC20615798. VBIAcaMar40141_0550.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAWEALDIG.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-630-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. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_ACAM1
AccessionPrimary (citable) accession number: B0CD95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways