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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: -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. Multifunctional fusion protein (pgk), Bifunctional PGK/TIM (pgk/tpi)
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. Multifunctional fusion protein (pgk), Bifunctional PGK/TIM (pgk/tpi)
  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 (Tmari_0206), 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)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

Keywordsi

Molecular functionIsomerase, Kinase, Multifunctional enzyme, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Gluconeogenesis, Glycolysis, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-382
BRENDAi5.3.1.1 6331
SABIO-RKiP36204
UniPathwayi
UPA00109;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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB04510 3-Phosphoglyceric Acid

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

3D structure databases

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
OMAiERRHIFQ

Family and domain databases

CDDicd00318 Phosphoglycerate_kinase, 1 hit
cd00311 TIM, 1 hit
Gene3Di3.20.20.70, 1 hit
3.40.50.1260, 2 hits
HAMAPiMF_00145 Phosphoglyc_kinase, 1 hit
MF_00147_B TIM_B, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR001576 Phosphoglycerate_kinase
IPR015911 Phosphoglycerate_kinase_CS
IPR015824 Phosphoglycerate_kinase_N
IPR036043 Phosphoglycerate_kinase_sf
IPR035990 TIM_sf
IPR022896 TrioseP_Isoase_bac/euk
IPR000652 Triosephosphate_isomerase
IPR020861 Triosephosphate_isomerase_AS
PANTHERiPTHR11406 PTHR11406, 1 hit
PfamiView protein in Pfam
PF00162 PGK, 1 hit
PF00121 TIM, 1 hit
PRINTSiPR00477 PHGLYCKINASE
SUPFAMiSSF51351 SSF51351, 1 hit
SSF53748 SSF53748, 1 hit
TIGRFAMsiTIGR00419 tim, 1 hit
PROSITEiView protein in PROSITE
PS00111 PGLYCERATE_KINASE, 1 hit
PS00171 TIM_1, 1 hit
PS51440 TIM_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPGKT_THEMA
AccessioniPrimary (citable) accession number: P36204
Secondary accession number(s): Q60031
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: April 25, 2018
This is version 139 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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