Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A4SH15 (PGK_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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

Protein attributes

Sequence length397 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 – 397397Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000076598

Regions

Nucleotide binding354 – 3574ATP By similarity
Region21 – 233Substrate binding By similarity
Region60 – 634Substrate binding By similarity

Sites

Binding site371Substrate By similarity
Binding site1191Substrate By similarity
Binding site1521Substrate By similarity
Binding site2031ATP By similarity
Binding site2941ATP; via carbonyl oxygen By similarity
Binding site3251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SH15 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: F3B5B684AD5A1F6C

FASTA39742,406
        10         20         30         40         50         60 
MQKKTLSDIT IQGKRILMRV DFNVPLNDER EITDDKRIVE ALPSIRKILD NGGRLILMSH 

        70         80         90        100        110        120 
LGRPKGKVNP IFSLAPVAAK LSELIDTPVA MAEDCIGTEV MQSALALQDG EVMLLENLRF 

       130        140        150        160        170        180 
HPEEEANDPE FAKELAALGE MYVNDAFGTA HRAHASTEGI THFVPTAVAG YLIEKELMYL 

       190        200        210        220        230        240 
GKALEKPERP FVAILGGSKI SGKIDVLENL FKKVDTVLIG GAMVFTFFKA MGLETGSSLV 

       250        260        270        280        290        300 
EDNKLELALS LLEQAKNRNI KLLLPQDVIA APELSADAPF HAVSVKELEA GEMGLDIGPL 

       310        320        330        340        350        360 
TIEAYRQEIL GARTILWNGP MGVFEIDSFA NGTFAVAEAM ALATAKGATT IIGGGDSAAA 

       370        380        390 
VAKAGLASKM THISTGGGAS LEFLEGKELP GIAALND 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37774.1.
RefSeqYP_001131276.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SH15.
SMRA4SH15. Positions 1-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1766.

Proteomic databases

PRIDEA4SH15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37774; ABP37774; Cvib_1766.
GeneID4971306.
KEGGpvi:Cvib_1766.
PATRIC21398084. VBIChlPha132153_1858.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAFPVDYVT.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1816-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.
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.
ProtoNetSearch...

Entry information

Entry namePGK_PROVI
AccessionPrimary (citable) accession number: A4SH15
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: June 11, 2014
This is version 48 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