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Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathway:iglycolysis

This protein is involved in step 2 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361SubstrateBy similarity
Binding sitei118 – 1181SubstrateBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Binding sitei201 – 2011ATPBy similarity
Binding sitei323 – 3231ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi350 – 3534ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33930-MONOMER.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
Gene namesi
Name:pgk
Ordered Locus Names:BSU33930
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU33930. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Phosphoglycerate kinasePRO_0000145905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphoserine1 Publication
Modified residuei299 – 2991Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP40924.
PRIDEiP40924.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018401.

Structurei

3D structure databases

ProteinModelPortaliP40924.
SMRiP40924. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 233Substrate bindingBy similarity
Regioni59 – 624Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0126.
HOGENOMiHOG000227108.
InParanoidiP40924.
KOiK00927.
OMAiWEALDIG.
OrthoDBiEOG64N9Z0.
PhylomeDBiP40924.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKKTLKDID VKGKVVFCRV DFNVPMKDGE VTDDTRIRAA LPTIKHLADQ
60 70 80 90 100
GAKVLLASHL GRPKGEVVEE LRLTPVAARL GELLGKEVKK ADEAYGDAVK
110 120 130 140 150
AQISEMKDGD VLVLENVRFY PGEEKNDPEL AKAFAELADV YVNDAFGAAH
160 170 180 190 200
RAHASTAGIA EHLPAVAGFL MEKELDVLGK AVSNPDRPFT AIIGGAKVKD
210 220 230 240 250
KIGVIESLLD KVDNLIIGGG LAYTFVKALG YEVGKSLLEE DKIELAKSFM
260 270 280 290 300
DRAKEKGVNF YMPEDVLVAD DFSNDANVKI VPISEIPSDL EAIDIGTKTR
310 320 330 340 350
ETYADVIKNS KLVVWNGPMG VFEIDLFAQG TKAVAEALAE AKDTYSVIGG
360 370 380 390
GDSAAAVEKF GLADKMSHIS TGGGASLEFM EGKELPGVAA LNDK
Length:394
Mass (Da):42,190
Last modified:July 15, 1998 - v3
Checksum:iC909AF1D76AF0F83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881V → A in AAA21678 (PubMed:8021172).Curated
Sequence conflicti393 – 3942DK → R in AAA21678 (PubMed:8021172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15398.1.
L29475 Genomic DNA. Translation: AAA21678.1.
PIRiC69675.
RefSeqiNP_391273.1. NC_000964.3.
WP_003243051.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15398; CAB15398; BSU33930.
GeneIDi938572.
KEGGibsu:BSU33930.
PATRICi18978786. VBIBacSub10457_3556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15398.1.
L29475 Genomic DNA. Translation: AAA21678.1.
PIRiC69675.
RefSeqiNP_391273.1. NC_000964.3.
WP_003243051.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP40924.
SMRiP40924. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018401.

Proteomic databases

PaxDbiP40924.
PRIDEiP40924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15398; CAB15398; BSU33930.
GeneIDi938572.
KEGGibsu:BSU33930.
PATRICi18978786. VBIBacSub10457_3556.

Organism-specific databases

GenoListiBSU33930. [Micado]

Phylogenomic databases

eggNOGiCOG0126.
HOGENOMiHOG000227108.
InParanoidiP40924.
KOiK00927.
OMAiWEALDIG.
OrthoDBiEOG64N9Z0.
PhylomeDBiP40924.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
BioCyciBSUB:BSU33930-MONOMER.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Identification of vegetative proteins for a two-dimensional protein index of Bacillus subtilis."
    Schmid R., Bernhardt J., Antelmann H., Voelker U., Mach H., Voelker A., Hecker M.
    Microbiology 143:991-998(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-23.
    Strain: 168 / IS58.
  3. "Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis."
    Leyva-Vazquez M.A., Setlow P.
    J. Bacteriol. 176:3903-3910(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-394.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  4. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND THR-299, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiPGK_BACSU
AccessioniPrimary (citable) accession number: P40924
Secondary accession number(s): O32252
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.