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Q1IZA3 (PGK_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Dgeo_1134
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length389 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_processglycolysis

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 – 389389Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096336

Regions

Nucleotide binding347 – 3504ATP By similarity
Region19 – 213Substrate binding By similarity
Region57 – 604Substrate binding By similarity

Sites

Binding site341Substrate By similarity
Binding site1171Substrate By similarity
Binding site1501Substrate By similarity
Binding site2001ATP By similarity
Binding site2881ATP; via carbonyl oxygen By similarity
Binding site3191ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IZA3 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: DEB26BF53FDA12E9

FASTA38941,491
        10         20         30         40         50         60 
MQTLDQLDVN GKRVLVRVDY NVPIKDGVVQ DETRVTASLP TLQHLLARGA ALVLLSHLGR 

        70         80         90        100        110        120 
PKNGPEEKYS LRPVAAVLER ALGRPVKFIA SLPSSEETRR AVESLQPGEV ALLENVRFEP 

       130        140        150        160        170        180 
GEEKNDPELV EQLARLGDAF VLDAFGSAHR AHASVSGVAG RLPHAAGLLL HNEVEALSRL 

       190        200        210        220        230        240 
LHDPARPYVV IIGGAKVSDK IKVIENLLPR VDRMLIGGGM MFTFIRARGG QIGNSLVEED 

       250        260        270        280        290        300 
QVAYARQLLE QYGDRLMLPT DAVAADRFAP DAQTRVVPAD RIPDGWMGLD IGPETARAYA 

       310        320        330        340        350        360 
EALQGAKTVF WNGPMGVFEF PAFAAGTNAV AQAVAELGNQ AYTVVGGGDS VSAINQSGQA 

       370        380 
SKVSHISTGG GASLELLEGQ LLPGVEAMK 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF45431.1.
RefSeqYP_604600.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IZA3.
SMRQ1IZA3. Positions 1-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_1134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF45431; ABF45431; Dgeo_1134.
GeneID4058302.
KEGGdge:Dgeo_1134.
PATRIC21624153. VBIDeiGeo41128_1713.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-1156-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_DEIGD
AccessionPrimary (citable) accession number: Q1IZA3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 58 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