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P18912

- PGK_GEOSE

UniProt

P18912 - PGK_GEOSE

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Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361SubstrateBy similarity
Binding sitei118 – 1181SubstrateBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Binding sitei201 – 2011ATP
Binding sitei316 – 3161ATP
Binding sitei323 – 3231ATP

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP18912.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
Gene namesi
Name:pgk
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Phosphoglycerate kinasePRO_0000145904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei299 – 2991PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi15 – 195Combined sources
Beta strandi30 – 323Combined sources
Helixi35 – 4915Combined sources
Beta strandi53 – 575Combined sources
Helixi69 – 713Combined sources
Helixi74 – 8411Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 1048Combined sources
Beta strandi111 – 1133Combined sources
Helixi117 – 1193Combined sources
Helixi122 – 1254Combined sources
Helixi128 – 1358Combined sources
Beta strandi139 – 1435Combined sources
Helixi146 – 1483Combined sources
Turni154 – 1574Combined sources
Helixi158 – 1614Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 18315Combined sources
Beta strandi187 – 1937Combined sources
Helixi198 – 20811Combined sources
Turni209 – 2113Combined sources
Beta strandi213 – 2175Combined sources
Helixi221 – 2288Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 25614Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 27310Combined sources
Beta strandi278 – 2825Combined sources
Helixi283 – 2853Combined sources
Beta strandi291 – 2955Combined sources
Helixi297 – 30812Combined sources
Beta strandi311 – 3177Combined sources
Helixi325 – 3273Combined sources
Helixi329 – 34012Combined sources
Beta strandi345 – 3484Combined sources
Helixi351 – 3599Combined sources
Helixi363 – 3653Combined sources
Beta strandi366 – 3694Combined sources
Helixi374 – 3807Combined sources
Helixi386 – 3894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHPX-ray1.65A1-394[»]
ProteinModelPortaliP18912.
SMRiP18912. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18912.

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

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.

P18912-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKKTIRDVD VRGKRVFCRV DFNVPMEQGA ITDDTRIRAA LPTIRYLIEH
60 70 80 90 100
GAKVILASHL GRPKGKVVEE LRLDAVAKRL GELLERPVAK TNEAVGDEVK
110 120 130 140 150
AAVDRLNEGD VLLLENVRFY PGEEKNDPEL AKAFAELADL YVNDAFGAAH
160 170 180 190 200
RAHASTEGIA HYLPAVAGFL MEKELEVLGK ALSNPDRPFT AIIGGAKVKD
210 220 230 240 250
KIGVIDNLLE KVDNLIIGGG LAYTFVKALG HDVGKSLLEE DKIELAKSFM
260 270 280 290 300
EKAKEKGVRF YMPVDVVVAD RFANDANTKV VPIDAIPADW SALDIGPKTR
310 320 330 340 350
ELYRDVIRES KLVVWNGPMG VFEMDAFAHG TKAIAEALAE ALDTYSVIGG
360 370 380 390
GDSAAAVEKF GLADKMDHIS TGGGASLEFM EGKQLPGVVA LEDK
Length:394
Mass (Da):42,730
Last modified:August 1, 1992 - v2
Checksum:i46BFA286F60E365A
GO

Sequence cautioni

The sequence AAA22462.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58059 Genomic DNA. Translation: CAA41093.1.
M24493 Genomic DNA. Translation: AAA22462.1. Different initiation.
PIRiJQ1399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58059 Genomic DNA. Translation: CAA41093.1 .
M24493 Genomic DNA. Translation: AAA22462.1 . Different initiation.
PIRi JQ1399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PHP X-ray 1.65 A 1-394 [» ]
ProteinModelPortali P18912.
SMRi P18912. Positions 1-394.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00185 .
SABIO-RK P18912.

Miscellaneous databases

EvolutionaryTracei P18912.

Family and domain databases

Gene3Di 3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPi MF_00145. Phosphoglyc_kinase.
InterProi IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view ]
PANTHERi PTHR11406. PTHR11406. 1 hit.
Pfami PF00162. PGK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000724. Pgk. 1 hit.
PRINTSi PR00477. PHGLYCKINASE.
SUPFAMi SSF53748. SSF53748. 1 hit.
PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus."
    Davies G.J., Littlechild J.A., Watson H.C., Hall L.
    Gene 109:39-45(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli."
    Branlant C., Oster T., Branlant G.
    Gene 75:145-155(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
  3. "Purification, crystallization and preliminary X-ray analysis of the 3-phosphoglycerate kinase from Bacillus stearothermophilus."
    Davies G.J., Gamblin S.J., Littlechild J.A., Watson H.C.
    J. Mol. Biol. 227:1263-1264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  4. "Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A."
    Davies G.J., Gamblin S.J., Littlechild J.A., Dauter Z., Wilson K.S., Watson H.C.
    Acta Crystallogr. D 50:202-209(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  5. "Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?"
    Hosszu L.L.P., Craven C.J., Spencer J., Parker M.J., Clarke A.R., Kelly M., Waltho J.P.
    Biochemistry 36:333-340(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-174 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiPGK_GEOSE
AccessioniPrimary (citable) accession number: P18912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3