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P36204

- PGKT_THEMA

UniProt

P36204 - PGKT_THEMA

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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: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate1 Publication
Binding sitei118 – 1181Substrate1 Publication
Binding sitei151 – 1511Substrate1 Publication
Binding sitei201 – 2011ATP
Binding sitei293 – 2931ATP; via carbonyl oxygen
Binding sitei317 – 3171ATP
Binding sitei324 – 3241ATP
Active sitei495 – 4951By similarity
Active sitei567 – 5671By similarity

Regions

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

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Bifunctional PGK/TIMPRO_0000146025Add
BLAST

Interactioni

Subunit structurei

Monomer (PGK) and homotetramer (PGK-TIM).2 Publications

Protein-protein interaction databases

STRINGi243274.TM0689.

Structurei

Secondary structure

1
654
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 strandi89 – 924Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 1048Combined sources
Beta strandi111 – 1144Combined 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
Turni219 – 2213Combined sources
Helixi222 – 2287Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 25513Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 2718Combined sources
Beta strandi279 – 2824Combined sources
Turni283 – 2853Combined sources
Beta strandi292 – 2965Combined sources
Helixi298 – 30811Combined sources
Beta strandi312 – 3187Combined sources
Helixi326 – 3283Combined sources
Helixi330 – 34415Combined sources
Beta strandi348 – 3536Combined sources
Helixi354 – 3629Combined sources
Helixi366 – 3683Combined sources
Beta strandi369 – 3746Combined sources
Helixi376 – 3838Combined sources
Helixi389 – 3924Combined sources
Beta strandi405 – 4095Combined sources
Helixi416 – 42914Combined sources
Beta strandi435 – 4417Combined sources
Helixi444 – 4463Combined sources
Helixi447 – 4548Combined sources
Beta strandi457 – 4648Combined sources
Beta strandi468 – 4736Combined sources
Helixi480 – 4845Combined sources
Turni485 – 4873Combined sources
Beta strandi490 – 4945Combined sources
Helixi496 – 5005Combined sources
Helixi506 – 51813Combined sources
Beta strandi522 – 5276Combined sources
Helixi531 – 5366Combined sources
Helixi539 – 55113Combined sources
Helixi556 – 5594Combined sources
Beta strandi563 – 5664Combined sources
Helixi569 – 5713Combined sources
Beta strandi572 – 5754Combined sources
Helixi580 – 59718Combined sources
Helixi600 – 6056Combined sources
Beta strandi606 – 6138Combined sources
Helixi616 – 6194Combined sources
Turni620 – 6223Combined sources
Beta strandi623 – 6253Combined sources
Beta strandi630 – 6345Combined sources
Helixi635 – 6373Combined sources
Helixi641 – 6499Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP36204.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 399399Phosphoglycerate kinaseAdd
BLAST
Regioni21 – 233Substrate binding
Regioni59 – 624Substrate binding
Regioni400 – 654255Triosephosphate isomeraseAdd
BLAST

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

eggNOGiCOG0149.
InParanoidiP36204.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131D → N in CAA53187. (PubMed:7859734)Curated
Sequence conflicti394 – 3963IAD → MRI(PubMed:7859734)Curated
Sequence conflicti626 – 6261K → R(PubMed:7859734)Curated
Sequence conflicti640 – 6401E → Q(PubMed:7859734)Curated

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.
YP_007977039.1. NC_021214.1.
YP_008990342.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35771; AAD35771; TM_0689.
GeneIDi18092100.
898356.
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 .
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:
PDBei
RCSB PDBi
PDBji
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 18092100.
898356.
KEGGi tma:TM0689.
PATRICi 23936296. VBITheMar51294_0701.

Phylogenomic databases

eggNOGi COG0149.
InParanoidi P36204.
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: November 26, 2014
This is version 118 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