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P36204

- PGKT_THEMA

UniProt

P36204 - PGKT_THEMA

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
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 4 (30 May 2000)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 116 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