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P36204

- PGKT_THEMA

UniProt

P36204 - PGKT_THEMA

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Protein

Bifunctional PGK/TIM

Gene
pgk/tpi, TM_0689
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - 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.UniRule annotation
D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate
Binding sitei118 – 1181Substrate
Binding sitei151 – 1511Substrate
Binding sitei201 – 2011ATP
Binding sitei293 – 2931ATP; via carbonyl oxygen
Binding sitei317 – 3171ATP
Binding sitei324 – 3241ATP
Active sitei495 – 4951 By similarity
Active sitei567 – 5671 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi353 – 3564ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate kinase activity Source: UniProtKB-EC
  3. triose-phosphate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. gluconeogenesis Source: UniProtKB-KW
  3. glycolytic process Source: UniProtKB-UniPathway
  4. pentose-phosphate shunt Source: UniProtKB-KW
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.
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
ProteomesiUP000008183: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Bifunctional PGK/TIMUniRule annotationPRO_0000146025Add
BLAST

Interactioni

Subunit structurei

Monomer (PGK) and homotetramer (PGK-TIM).1 Publication

Protein-protein interaction databases

STRINGi243274.TM0689.

Structurei

Secondary structure

1
654
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Beta strandi15 – 195
Beta strandi30 – 323
Helixi35 – 4915
Beta strandi53 – 575
Helixi69 – 713
Helixi74 – 8411
Beta strandi89 – 924
Beta strandi94 – 963
Helixi97 – 1048
Beta strandi111 – 1144
Helixi117 – 1193
Helixi122 – 1254
Helixi128 – 1358
Beta strandi139 – 1435
Helixi146 – 1483
Turni154 – 1574
Helixi158 – 1614
Beta strandi165 – 1673
Helixi169 – 18315
Beta strandi187 – 1937
Helixi198 – 20811
Turni209 – 2113
Beta strandi213 – 2175
Turni219 – 2213
Helixi222 – 2287
Helixi240 – 2423
Helixi243 – 25513
Beta strandi259 – 2613
Beta strandi264 – 2718
Beta strandi279 – 2824
Turni283 – 2853
Beta strandi292 – 2965
Helixi298 – 30811
Beta strandi312 – 3187
Helixi326 – 3283
Helixi330 – 34415
Beta strandi348 – 3536
Helixi354 – 3629
Helixi366 – 3683
Beta strandi369 – 3746
Helixi376 – 3838
Helixi389 – 3924
Beta strandi405 – 4095
Helixi416 – 42914
Beta strandi435 – 4417
Helixi444 – 4463
Helixi447 – 4548
Beta strandi457 – 4648
Beta strandi468 – 4736
Helixi480 – 4845
Turni485 – 4873
Beta strandi490 – 4945
Helixi496 – 5005
Helixi506 – 51813
Beta strandi522 – 5276
Helixi531 – 5366
Helixi539 – 55113
Helixi556 – 5594
Beta strandi563 – 5664
Helixi569 – 5713
Beta strandi572 – 5754
Helixi580 – 59718
Helixi600 – 6056
Beta strandi606 – 6138
Helixi616 – 6194
Turni620 – 6223
Beta strandi623 – 6253
Beta strandi630 – 6345
Helixi635 – 6373
Helixi641 – 6499

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9BX-ray2.85A/B400-654[»]
1VPEX-ray2.00A2-398[»]
ProteinModelPortaliP36204.
SMRiP36204. Positions 2-398, 400-653.

Miscellaneous databases

EvolutionaryTraceiP36204.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 399399Phosphoglycerate kinaseUniRule annotationAdd
BLAST
Regioni21 – 233Substrate bindingUniRule annotation
Regioni59 – 624Substrate bindingUniRule annotation
Regioni400 – 654255Triosephosphate isomeraseUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0149.
KOiK00927.
K01803.
OMAiDADEHEN.
OrthoDBiEOG64N9Z0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
MF_00147_B. TIM_B.
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

MEKMTIRDVD LKGKRVIMRV DFNVPVKDGV VQDDTRIRAA LPTIKYALEQ    50
GAKVILLSHL GRPKGEPSPE FSLAPVAKRL SELLGKEVKF VPAVVGDEVK 100
KAVEELKEGE VLLLENTRFH PGETKNDPEL AKFWASLADI HVNDAFGTAH 150
RAHASNVGIA QFIPSVAGFL MEKEIKFLSK VTYNPEKPYV VVLGGAKVSD 200
KIGVITNLME KADRILIGGA MMFTFLKALG KEVGSSRVEE DKIDLAKELL 250
EKAKEKGVEI VLPVDAVIAQ KIEPGVEKKV VRIDDGIPEG WMGLDIGPET 300
IELFKQKLSD AKTVVWNGPM GVFEIDDFAE GTKQVALAIA ALTEKGAITV 350
VGGGDSAAAV NKFGLEDKFS HVSTGGGASL EFLEGKELPG IASIADKKKI 400
TRKLILAGNW KMHKTISEAK KFVSLLVNEL HDVKEFEIVV CPPFTALSEV 450
GEILSGRNIK LGAQNVFYED QGAFTGEISP LMLQEIGVEY VIVGHSERRR 500
IFKEDDEFIN RKVKAVLEKG MTPILCVGET LEEREKGLTF CVVEKQVREG 550
FYGLDKEEAK RVVIAYEPVW AIGTGRVATP QQAQEVHAFI RKLLSEMYDE 600
ETAGSIRILY GGSIKPDNFL GLIVQKDIDG GLVGGASLKE SFIELARIMR 650
GVIS 654
Length:654
Mass (Da):71,585
Last modified:May 30, 2000 - v4
Checksum:i42358A4EF0C5E481
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131D → N in CAA53187. 1 Publication
Sequence conflicti394 – 3963IAD → MRI1 Publication
Sequence conflicti626 – 6261K → R1 Publication
Sequence conflicti640 – 6401E → Q1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_007977039.1. NC_021214.1.
YP_008990342.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35771; AAD35771; TM_0689.
GeneIDi898356.
KEGGitma:TM0689.
tmi:THEMA_01220.
tmm:Tmari_0689.
PATRICi23936296. VBITheMar51294_0701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75437 Genomic DNA. Translation: CAA53187.1 .
L27492 Genomic DNA. Translation: AAA67520.1 .
AE000512 Genomic DNA. Translation: AAD35771.1 .
PIRi G72344.
RefSeqi NP_228498.1. NC_000853.1.
YP_007977039.1. NC_021214.1.
YP_008990342.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B9B X-ray 2.85 A/B 400-654 [» ]
1VPE X-ray 2.00 A 2-398 [» ]
ProteinModelPortali P36204.
SMRi P36204. Positions 2-398, 400-653.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0689.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35771 ; AAD35771 ; TM_0689 .
GeneIDi 898356.
KEGGi tma:TM0689.
tmi:THEMA_01220.
tmm:Tmari_0689.
PATRICi 23936296. VBITheMar51294_0701.

Phylogenomic databases

eggNOGi COG0149.
KOi K00927.
K01803.
OMAi DADEHEN.
OrthoDBi EOG64N9Z0.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00185 .
UPA00109 ; UER00189 .
BioCyci MetaCyc:MONOMER-382.
SABIO-RK P36204.

Miscellaneous databases

EvolutionaryTracei P36204.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPi MF_00145. Phosphoglyc_kinase.
MF_00147_B. TIM_B.
InterProi IPR013785. 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 ]
PANTHERi PTHR11406. PTHR11406. 1 hit.
Pfami PF00162. PGK. 1 hit.
PF00121. TIM. 1 hit.
[Graphical view ]
PRINTSi PR00477. PHGLYCKINASE.
SUPFAMi SSF51351. SSF51351. 1 hit.
SSF53748. SSF53748. 1 hit.
TIGRFAMsi TIGR00419. tim. 1 hit.
PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphoglycerate kinase and triosephosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex."
    Schurig H., Beaucamp N., Ostendorp R., Jaenicke R., Adler E., Knowles J.R.
    EMBO J. 14:442-451(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability."
    Auerbach G., Huber R., Graettinger M., Zaiss K., Schurig H., Jaenicke R., Jacob U.
    Structure 5:1475-1483(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH SUBSTRATE AND ATP ANALOG, SEQUENCE REVISION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  4. "The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures."
    Maes D., Zeelen J.P., Thanki N., Beaucamp N., Alvarez M., Thi M.H., Backmann J., Martial J.A., Wyns L., Jaenicke R., Wierenga R.K.
    Proteins 37:441-453(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 400-654.

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: July 9, 2014
This is version 115 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

External Data

Dasty 3

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