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Reviewed, UniProtKB/Swiss-Prot P36204 (PGKT_THEMA)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bifunctional PGK/TIM
Including the following 2 domains:
    1- Recommended name:
            Phosphoglycerate kinase
              EC=2.7.2.3
    2- Recommended name:
            Triosephosphate isomerase
                Short name=TIM
              EC=5.3.1.1
        Alternative name(s):
            Triose-phosphate isomerase
Gene names
Name: pgk/tpi
Ordered Locus Names: TM_0689
OrganismThermotoga maritima [Complete proteome] [HAMAP]
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP MF_00145

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00145

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00145

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP MF_00145

Subunit structure

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

Subcellular location

Cytoplasm. HAMAP MF_00145

Sequence similarities

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

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Bifunctional PGK/TIM HAMAP MF_00145
PRO_0000146025

Regions

Nucleotide binding353 – 3564ATP HAMAP MF_00145
Region1 – 399399Phosphoglycerate kinase HAMAP MF_00145
Region21 – 233Substrate binding HAMAP MF_00145
Region59 – 624Substrate binding HAMAP MF_00145
Region400 – 654255Triosephosphate isomerase HAMAP MF_00145

Sites

Active site4951 By similarity
Active site5671 By similarity
Binding site361Substrate HAMAP MF_00145
Binding site1181Substrate HAMAP MF_00145
Binding site1511Substrate HAMAP MF_00145
Binding site2011ATP HAMAP MF_00145
Binding site2931ATP; via carbonyl oxygen HAMAP MF_00145
Binding site3171ATP HAMAP MF_00145
Binding site3241ATP HAMAP MF_00145

Experimental info

Sequence conflict2131D → N in CAA53187. Ref.1
Sequence conflict394 – 3963IAD → MRI Ref.1
Sequence conflict6261K → R Ref.1
Sequence conflict6401E → Q Ref.1

Secondary structure

1 ................................................................................................................................ 654
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P36204-1 [UniParc].

Last modified May 30, 2000. Version 4.
Checksum: 42358A4EF0C5E481

FASTA65471,585
        10         20         30         40         50         60 
MEKMTIRDVD LKGKRVIMRV DFNVPVKDGV VQDDTRIRAA LPTIKYALEQ GAKVILLSHL 

        70         80         90        100        110        120 
GRPKGEPSPE FSLAPVAKRL SELLGKEVKF VPAVVGDEVK KAVEELKEGE VLLLENTRFH 

       130        140        150        160        170        180 
PGETKNDPEL AKFWASLADI HVNDAFGTAH RAHASNVGIA QFIPSVAGFL MEKEIKFLSK 

       190        200        210        220        230        240 
VTYNPEKPYV VVLGGAKVSD KIGVITNLME KADRILIGGA MMFTFLKALG KEVGSSRVEE 

       250        260        270        280        290        300 
DKIDLAKELL EKAKEKGVEI VLPVDAVIAQ KIEPGVEKKV VRIDDGIPEG WMGLDIGPET 

       310        320        330        340        350        360 
IELFKQKLSD AKTVVWNGPM GVFEIDDFAE GTKQVALAIA ALTEKGAITV VGGGDSAAAV 

       370        380        390        400        410        420 
NKFGLEDKFS HVSTGGGASL EFLEGKELPG IASIADKKKI TRKLILAGNW KMHKTISEAK 

       430        440        450        460        470        480 
KFVSLLVNEL HDVKEFEIVV CPPFTALSEV GEILSGRNIK LGAQNVFYED QGAFTGEISP 

       490        500        510        520        530        540 
LMLQEIGVEY VIVGHSERRR IFKEDDEFIN RKVKAVLEKG MTPILCVGET LEEREKGLTF 

       550        560        570        580        590        600 
CVVEKQVREG FYGLDKEEAK RVVIAYEPVW AIGTGRVATP QQAQEVHAFI RKLLSEMYDE 

       610        620        630        640        650 
ETAGSIRILY GGSIKPDNFL GLIVQKDIDG GLVGGASLKE SFIELARIMR GVIS

« Hide

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References

« Hide 'large scale' references
[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: 7859734] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
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: 9384563] [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: 10591103] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 400-654.

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Cross-references

Sequence databases

X75437 Genomic DNA. Translation: CAA53187.1.
L27492 Genomic DNA. Translation: AAA67520.1.
AE000512 Genomic DNA. Translation: AAD35771.1.
PIRG72344.
RefSeqNP_228498.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B9BX-ray2.85A/B400-654[»]
1VPEX-ray2.00A2-393[»]
ModBaseSearch...

Genome annotation databases

GeneID898356.
GenomeReviewsGene locus TM_0689 in contig AE000512_GR.
KEGGtma:TM0689.
NMPDRfig|243274.1.peg.682.
TIGRTM_0689.

Phylogenomic databases

HOGENOMP36204.
OMAP36204. ILAGNWK.

Enzyme and pathway databases

BioCycMetaCyc:MON-382.
TMAR243274:TM_0689-MON.
BRENDA2.7.2.3. 16699.
5.3.1.1. 16699.

Family and domain databases

HAMAPMF_00145. Fused.
[Tree]
MF_00147. Fused.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001576. Phosphoglycerate_kinase.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
IPR000652. Triosephosphate_isomerase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.
PANTHERPTHR11406. PGK. 1 hit.
PfamPF00162. PGK. 1 hit.
PF00121. TIM. 1 hit.
[Graphical view]
PRINTSPR00477. PHGLYCKINASE.
ProDomPD001005. Triophos_ismrse. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePGKT_THEMA
AccessionPrimary (citable) accession number: P36204
Secondary accession number(s): Q60031
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: June 16, 2009
This is version 80 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents