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Protein

Bifunctional PGK/TIM

Gene

pgk/tpi

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional PGK/TIM (pgk/tpi), Phosphoglycerate kinase (Tmari_0689)
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 D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Pathwayi: glycolysis

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 (gap)
  2. Bifunctional PGK/TIM (pgk/tpi), Phosphoglycerate kinase (Tmari_0689)
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
  4. Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (Tmari_0206)
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)DescriptionActionsGraphical viewLength
Binding sitei36Substrate1 Publication1
Binding sitei118Substrate1 Publication1
Binding sitei151Substrate1 Publication1
Binding sitei201ATP1
Binding sitei293ATP; via carbonyl oxygen1
Binding sitei317ATP1
Binding sitei324ATP1
Active sitei495ElectrophileUniRule annotation1
Active sitei567Proton acceptorUniRule annotation1
Binding sitei572Substrate; via amide nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi353 – 356ATP4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Kinase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Gluconeogenesis, Glycolysis, Lipid biosynthesis, Lipid metabolism, Pentose shunt

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-382.
BRENDAi5.3.1.1. 6331.
SABIO-RKP36204.
UniPathwayiUPA00109; UER00185.
UPA00109; UER00189.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional PGK/TIM
Including the following 2 domains:
Phosphoglycerate kinase (EC:2.7.2.3)
Triosephosphate isomerase (EC:5.3.1.1)
Short name:
TIM
Alternative name(s):
Triose-phosphate isomerase
Gene namesi
Name:pgk/tpi
Ordered Locus Names:TM_0689
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001460251 – 654Bifunctional PGK/TIMAdd BLAST654

Interactioni

Subunit structurei

Monomer (PGK) and homotetramer (PGK-TIM).3 Publications

Protein-protein interaction databases

STRINGi243274.TM0689.

Structurei

Secondary structure

1654
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Beta strandi15 – 19Combined sources5
Beta strandi30 – 32Combined sources3
Helixi35 – 49Combined sources15
Beta strandi53 – 57Combined sources5
Helixi69 – 71Combined sources3
Helixi74 – 84Combined sources11
Beta strandi89 – 92Combined sources4
Beta strandi94 – 96Combined sources3
Helixi97 – 104Combined sources8
Beta strandi111 – 114Combined sources4
Helixi117 – 119Combined sources3
Helixi122 – 125Combined sources4
Helixi128 – 135Combined sources8
Beta strandi139 – 143Combined sources5
Helixi146 – 148Combined sources3
Turni154 – 157Combined sources4
Helixi158 – 161Combined sources4
Beta strandi165 – 167Combined sources3
Helixi169 – 183Combined sources15
Beta strandi187 – 193Combined sources7
Helixi198 – 208Combined sources11
Turni209 – 211Combined sources3
Beta strandi213 – 217Combined sources5
Turni219 – 221Combined sources3
Helixi222 – 228Combined sources7
Helixi240 – 242Combined sources3
Helixi243 – 255Combined sources13
Beta strandi259 – 261Combined sources3
Beta strandi264 – 271Combined sources8
Beta strandi279 – 282Combined sources4
Turni283 – 285Combined sources3
Beta strandi292 – 296Combined sources5
Helixi298 – 308Combined sources11
Beta strandi312 – 318Combined sources7
Helixi326 – 328Combined sources3
Helixi330 – 344Combined sources15
Beta strandi348 – 353Combined sources6
Helixi354 – 362Combined sources9
Helixi366 – 368Combined sources3
Beta strandi369 – 374Combined sources6
Helixi376 – 383Combined sources8
Helixi389 – 392Combined sources4
Beta strandi405 – 409Combined sources5
Helixi416 – 429Combined sources14
Beta strandi435 – 441Combined sources7
Helixi444 – 446Combined sources3
Helixi447 – 454Combined sources8
Beta strandi457 – 464Combined sources8
Beta strandi468 – 473Combined sources6
Helixi480 – 484Combined sources5
Turni485 – 487Combined sources3
Beta strandi490 – 494Combined sources5
Helixi496 – 500Combined sources5
Helixi506 – 518Combined sources13
Beta strandi522 – 527Combined sources6
Helixi531 – 536Combined sources6
Helixi539 – 551Combined sources13
Helixi556 – 559Combined sources4
Beta strandi563 – 566Combined sources4
Helixi569 – 571Combined sources3
Beta strandi572 – 575Combined sources4
Helixi580 – 597Combined sources18
Helixi600 – 605Combined sources6
Beta strandi606 – 613Combined sources8
Helixi616 – 619Combined sources4
Turni620 – 622Combined sources3
Beta strandi623 – 625Combined sources3
Beta strandi630 – 634Combined sources5
Helixi635 – 637Combined sources3
Helixi641 – 649Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9BX-ray2.85A/B400-654[»]
1VPEX-ray2.00A2-398[»]
ProteinModelPortaliP36204.
SMRiP36204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36204.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 399Phosphoglycerate kinaseAdd BLAST399
Regioni21 – 23Substrate binding3
Regioni59 – 62Substrate binding4
Regioni400 – 654Triosephosphate isomeraseAdd BLAST255
Regioni409 – 411Substrate bindingUniRule annotation3
Regioni634 – 635Substrate bindingUniRule annotation2

Sequence similaritiesi

In the N-terminal section; belongs to the phosphoglycerate kinase family.Curated
In the C-terminal section; belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4105BZA. Bacteria.
COG0126. LUCA.
COG0149. LUCA.
InParanoidiP36204.
KOiK00927.
K01803.
OMAiHYTHLEA.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
cd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
MF_00147_B. TIM_B. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
PF00121. TIM. 1 hit.
[Graphical view]
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF51351. SSF51351. 1 hit.
SSF53748. SSF53748. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36204-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKMTIRDVD LKGKRVIMRV DFNVPVKDGV VQDDTRIRAA LPTIKYALEQ
60 70 80 90 100
GAKVILLSHL GRPKGEPSPE FSLAPVAKRL SELLGKEVKF VPAVVGDEVK
110 120 130 140 150
KAVEELKEGE VLLLENTRFH PGETKNDPEL AKFWASLADI HVNDAFGTAH
160 170 180 190 200
RAHASNVGIA QFIPSVAGFL MEKEIKFLSK VTYNPEKPYV VVLGGAKVSD
210 220 230 240 250
KIGVITNLME KADRILIGGA MMFTFLKALG KEVGSSRVEE DKIDLAKELL
260 270 280 290 300
EKAKEKGVEI VLPVDAVIAQ KIEPGVEKKV VRIDDGIPEG WMGLDIGPET
310 320 330 340 350
IELFKQKLSD AKTVVWNGPM GVFEIDDFAE GTKQVALAIA ALTEKGAITV
360 370 380 390 400
VGGGDSAAAV NKFGLEDKFS HVSTGGGASL EFLEGKELPG IASIADKKKI
410 420 430 440 450
TRKLILAGNW KMHKTISEAK KFVSLLVNEL HDVKEFEIVV CPPFTALSEV
460 470 480 490 500
GEILSGRNIK LGAQNVFYED QGAFTGEISP LMLQEIGVEY VIVGHSERRR
510 520 530 540 550
IFKEDDEFIN RKVKAVLEKG MTPILCVGET LEEREKGLTF CVVEKQVREG
560 570 580 590 600
FYGLDKEEAK RVVIAYEPVW AIGTGRVATP QQAQEVHAFI RKLLSEMYDE
610 620 630 640 650
ETAGSIRILY GGSIKPDNFL GLIVQKDIDG GLVGGASLKE SFIELARIMR

GVIS
Length:654
Mass (Da):71,585
Last modified:May 30, 2000 - v4
Checksum:i42358A4EF0C5E481
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213D → N in CAA53187 (PubMed:7859734).Curated1
Sequence conflicti394 – 396IAD → MRI in CAA53187 (PubMed:7859734).Curated3
Sequence conflicti626K → R in CAA53187 (PubMed:7859734).Curated1
Sequence conflicti640E → Q in CAA53187 (PubMed:7859734).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75437 Genomic DNA. Translation: CAA53187.1.
L27492 Genomic DNA. Translation: AAA67520.1.
AE000512 Genomic DNA. Translation: AAD35771.1.
PIRiG72344.
RefSeqiNP_228498.1. NC_000853.1.
WP_004081072.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35771; AAD35771; TM_0689.
GeneIDi898356.
KEGGitma:TM0689.
PATRICi23936296. VBITheMar51294_0701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75437 Genomic DNA. Translation: CAA53187.1.
L27492 Genomic DNA. Translation: AAA67520.1.
AE000512 Genomic DNA. Translation: AAD35771.1.
PIRiG72344.
RefSeqiNP_228498.1. NC_000853.1.
WP_004081072.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9BX-ray2.85A/B400-654[»]
1VPEX-ray2.00A2-398[»]
ProteinModelPortaliP36204.
SMRiP36204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35771; AAD35771; TM_0689.
GeneIDi898356.
KEGGitma:TM0689.
PATRICi23936296. VBITheMar51294_0701.

Phylogenomic databases

eggNOGiENOG4105BZA. Bacteria.
COG0126. LUCA.
COG0149. LUCA.
InParanoidiP36204.
KOiK00927.
K01803.
OMAiHYTHLEA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
UPA00109; UER00189.
BioCyciMetaCyc:MONOMER-382.
BRENDAi5.3.1.1. 6331.
SABIO-RKP36204.

Miscellaneous databases

EvolutionaryTraceiP36204.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
cd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
MF_00147_B. TIM_B. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
PF00121. TIM. 1 hit.
[Graphical view]
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF51351. SSF51351. 1 hit.
SSF53748. SSF53748. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGKT_THEMA
AccessioniPrimary (citable) accession number: P36204
Secondary accession number(s): Q60031
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

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

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 one 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.