Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2RLU1 (PGK_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. 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
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:Moth_0263
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella ›

Protein attributes

Sequence length393 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.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference 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 – 393393Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058017

Regions

Nucleotide binding349 – 3524ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1181Substrate By similarity
Binding site1511Substrate By similarity
Binding site2011ATP By similarity
Binding site3231ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RLU1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: CB26BFEB04319DD8

FASTA39341,633
        10         20         30         40         50         60 
MAKLTLKDLE LNNKRVLVRV DFNVPLEAGR VTDNTRIRAA LPTIEYLLDH GARVILMSHL 

        70         80         90        100        110        120 
GRPKGKVKEE LRLDPVAREL ESLLGRQVHK VNDCVGPEVE AAAAALKPGE VLLLENLRFH 

       130        140        150        160        170        180 
PEEEKNDPGF ARQLASLADV YVNDAFGAAH RAHASTEGVA HYLPAAAGFL LQKEIETLGK 

       190        200        210        220        230        240 
ALADPERPFV AIIGGAKVSD KISVIRNLLT KVDTLIIGGG MANTFLKAQG YAMGKSLVEE 

       250        260        270        280        290        300 
DQVPLAQELI QLAAQKGVKM LLPRDLVVAQ EFKADAPHQV VAVNAVPDGW MALDIGPETA 

       310        320        330        340        350        360 
RAYAGALEGA RTVVWNGPMG VFEMEAFAHG TEAVARAVAA VDGMTIVGGG DSVAAVEKMG 

       370        380        390 
VAGKIGHIST GGGASLEFLE GKALPGVVAL TEK

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000232 Genomic DNA. Translation: ABC18598.1.
RefSeqYP_429141.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RLU1.
SMRQ2RLU1. Positions 1-393.
ModBaseSearch...

Protein-protein interaction databases

STRING264732.Moth_0263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC18598; ABC18598; Moth_0263.
GeneID3833077.
KEGGmta:Moth_0263.
PATRIC22637559. VBIMooThe6753_0280.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAEKKNDEA.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-355-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_MOOTA
AccessionPrimary (citable) accession number: Q2RLU1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 24, 2006
Last modified: May 1, 2013
This is version 52 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents