DB code: T00239
| RLCP classification | 8.131.42001.6 : Isomerization | |
|---|---|---|
| 8.113.42001.5 : Isomerization | ||
| CATH domain | 3.40.50.1260 : Rossmann fold | Catalytic domain |
| 3.40.50.1270 : Rossmann fold | Catalytic domain | |
| 3.20.20.70 : TIM Barrel | Catalytic domain | |
| E.C. | 2.7.2.3 5.3.1.1 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.20.20.70 : TIM Barrel | S00215 S00217 S00218 S00219 S00532 S00198 S00220 S00745 S00537 S00538 S00539 S00826 S00841 S00235 S00239 S00240 S00243 S00244 S00199 S00200 S00201 S00221 S00222 S00847 S00224 S00225 S00226 D00014 D00029 M00141 T00015 D00664 D00665 D00804 D00863 T00089 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Includes | RefSeq | Pfam |
|---|---|---|---|---|---|
| P36204 |
Bifunctional PGK/TIM
|
None |
Phosphoglycerate kinase
EC 2.7.2.3 Triosephosphate isomerase (TIM) EC 5.3.1.1 Triose-phosphate isomerase |
NP_228498.1
(Protein)
NC_000853.1 (DNA/RNA sequence) |
PF00162
(PGK)
PF00121 (TIM) [Graphical View] |
| KEGG enzyme name |
|---|
|
phosphoglycerate kinase
(EC 2.7.2.3 ) PGK (EC 2.7.2.3 ) 3-PGK (EC 2.7.2.3 ) ATP-3-phospho-D-glycerate-1-phosphotransferase (EC 2.7.2.3 ) ATP:D-3-phosphoglycerate 1-phosphotransferase (EC 2.7.2.3 ) 3-phosphoglycerate kinase (EC 2.7.2.3 ) 3-phosphoglycerate phosphokinase (EC 2.7.2.3 ) 3-phosphoglyceric acid kinase (EC 2.7.2.3 ) 3-phosphoglyceric acid phosphokinase (EC 2.7.2.3 ) 3-phosphoglyceric kinase (EC 2.7.2.3 ) glycerate 3-phosphate kinase (EC 2.7.2.3 ) glycerophosphate kinase (EC 2.7.2.3 ) phosphoglyceric acid kinase (EC 2.7.2.3 ) phosphoglyceric kinase (EC 2.7.2.3 ) phosphoglycerokinase (EC 2.7.2.3 ) triose-phosphate isomerase (EC 5.3.1.1 ) phosphotriose isomerase (EC 5.3.1.1 ) triose phosphoisomerase (EC 5.3.1.1 ) triose phosphate mutase (EC 5.3.1.1 ) D-glyceraldehyde-3-phosphate ketol-isomerase (EC 5.3.1.1 ) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P36204 | PGKT_THEMA | ATP + 3-phospho-D-glycerate = ADP + 3-phospho- D-glyceroyl phosphate. D-glyceraldehyde 3-phosphate = glycerone phosphate. | Monomer (PGK) and homotetramer (PGK-TIM). | Cytoplasm. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00010 | Glycolysis / Gluconeogenesis | 2.7.2.3 5.3.1.1 |
| MAP00031 | Inositol metabolism | 5.3.1.1 |
| MAP00051 | Fructose and mannose metabolism | 5.3.1.1 |
| MAP00710 | Carbon fixation in photosynthetic organisms | 2.7.2.3 5.3.1.1 |
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C00305 | C00002 | C00197 | C00118 | C00008 | C00236 | C00111 | I00178 | |||||
| E.C. |
2.7.2.3
|
2.7.2.3
|
2.7.2.3
|
5.3.1.1
|
2.7.2.3
|
2.7.2.3
|
5.3.1.1
|
5.3.1.1
|
|||||
| Compound | Magnesium | ATP | 3-Phospho-D-glycerate | D-Glyceraldehyde 3-phosphate | ADP | 3-Phospho-D-glyceroyl phosphate | Glycerone phosphate | Enediol form of glycerone phosphate | |||||
| Type | divalent metal (Ca2+, Mg2+) | amine group,nucleotide | carbohydrate,carboxyl group,phosphate group/phosphate ion | carbohydrate,phosphate group/phosphate ion | amine group,nucleotide | carbohydrate,phosphate group/phosphate ion | carbohydrate,phosphate group/phosphate ion | ||||||
| ChEBI |
18420 18420 |
15422 15422 |
17794 17794 |
29052 29052 |
16761 16761 |
16001 16001 |
16108 16108 |
||||||
| PubChem |
888 888 |
5957 5957 |
439183 439183 |
439168 439168 |
6022 6022 |
439191 439191 |
668 668 |
||||||
| 1vpeA01 |
|
|
|
|
|
Unbound | Unbound | Bound:3PG | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1vpeA02 |
|
|
|
|
|
Bound:_MG | Analogue:ANP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1b9bA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1b9bB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P36204, literature [3], [4], [6], [7] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1vpeA01 |
|
|
|
|
|
ARG 36 | ||||
| 1vpeA02 |
|
|
|
|
|
LYS 201;ASN 317 | ASP 355 | GLY 354;GLY 377 | ||
| 1b9bA |
|
|
|
|
|
ASN 10;LYS 12;HIS 96;GLU 168 | ||||
| 1b9bB |
|
|
|
|
|
ASN 510;LYS 512;HIS 596;GLU 668 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[4]
|
p.4431-4435 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9165089 |
| Journal | Biol Chem |
| Year | 1997 |
| Volume | 378 |
| Pages | 327-9 |
| Authors | Auerbach G, Jacob U, Grattinger M, Schurig H, Jaenicke R |
| Title | Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9278147 |
| Journal | Biol Chem |
| Year | 1997 |
| Volume | 378 |
| Pages | 679-85 |
| Authors | Beaucamp N, Schurig H, Jaenicke R |
| Title | The PGK-TIM fusion protein from Thermotoga maritima and its constituent parts are intrinsically stable and fold independently. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, |
| Medline ID | 98046096 |
| PubMed ID | 9384563 |
| Journal | Structure |
| Year | 1997 |
| Volume | 5 |
| Pages | 1475-83 |
| Authors | Auerbach G, Huber R, Grattinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U |
| Title | Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. |
| Related PDB | 1vpe |
| Related UniProtKB | P36204 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9521762 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 4429-36 |
| Authors | Bernstein BE, Hol WG |
| Title | Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | 99315861 |
| PubMed ID | 10383424 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 19181-7 |
| Authors | Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA |
| Title | Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF TIM. |
| Medline ID | 20058648 |
| PubMed ID | 10591103 |
| Journal | Proteins |
| Year | 1999 |
| Volume | 37 |
| Pages | 441-53 |
| Authors | Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK |
| Title | The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. |
| Related PDB | 1b9b |
| Related UniProtKB | P36204 |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11243785 |
| Journal | J Mol Biol |
| Year | 2001 |
| Volume | 306 |
| Pages | 745-57 |
| Authors | Walden H, Bell GS, Russell RJ, Siebers B, Hensel R, Taylor GL |
| Title |
Tiny TIM: a small, |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11265486 |
| Journal | Methods Enzymol |
| Year | 2001 |
| Volume | 331 |
| Pages | 90-104 |
| Authors | Crowhurst G, McHarg J, Littlechild JA |
| Title | Phosphoglycerate kinases from bacteria and archaea. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12102622 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 8796-806 |
| Authors | Kovari Z, Flachner B, Naray-Szabo G, Vas M |
| Title | Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14997553 |
| Journal | Proteins |
| Year | 2004 |
| Volume | 55 |
| Pages | 198-209 |
| Authors | Kovari Z, Vas M |
| Title | Protein conformer selection by sequence-dependent packing contacts in crystals of 3-phosphoglycerate kinase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme is composed of the N-terminal phosphoglycerate kinase (E.C. The N-terminal phosphoglycerate kinase domains (swiss-prot;P36204 residues 2-399) are homologous to those of the counterpart enzyme (D00125 in EzCatDB), Since the catalytic residues are conserved in both the domains, (A) Transfer of phosphoryl group from ATP to carboxyl oxygen (N-terminal domains): (B) Isomerization; Shift of double-bond from carbonyl group to adjacent C=C (C-terminal domain): (C) Isomerization; Shift of double-bond from C=C to carbonyl group (C-terminal domain): |
| Created | Updated |
|---|---|
| 2006-01-24 | 2014-07-08 |