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P50921 (TPIS_VIBMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Triosephosphate isomerase

Short name=TIM
EC=5.3.1.1
Alternative name(s):
Triose-phosphate isomerase
Gene names
Name:tpiA
Synonyms:tim, tpi
OrganismVibrio marinus (Moritella marina)
Taxonomic identifier90736 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147_B

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147_B

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147_B

Subunit structure

Homodimer. Ref.1

Subcellular location

Cytoplasm Probable HAMAP MF_00147_B.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Triosephosphate isomerase HAMAP MF_00147_B
PRO_0000090314

Sites

Active site971Electrophile
Active site1691Proton acceptor
Binding site91Substrate By similarity
Binding site111Substrate

Secondary structure

................................................... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50921 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5CC4BB8CFF27070A

FASTA25626,740
        10         20         30         40         50         60 
MRHPVVMGNW KLNGSKEMVV DLLNGLNAEL EGVTGVDVAV APPALFVDLA ERTLTEAGSA 

        70         80         90        100        110        120 
IILGAQNTDL NNSGAFTGDM SPAMLKEFGA THIIIGHSER REYHAESDEF VAKKFAFLKE 

       130        140        150        160        170        180 
NGLTPVLCIG ESDAQNEAGE TMAVCARQLD AVINTQGVEA LEGAIIAYEP IWAIGTGKAA 

       190        200        210        220        230        240 
TAEDAQRIHA QIRAHIAEKS EAVAKNVVIQ YGGSVKPENA AAYFAQPDID GALVGGAALD 

       250 
AKSFAAIAKA AAEAKA 

« Hide

References

[1]"Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties."
Alvarez M., Zeelen J.P., Mainfroid V., Rentier-Delrue F., Martial J.A., Wyns L., Wierenga R.K., Maes D.
J. Biol. Chem. 273:2199-2206(1998) [PubMed: 9442062] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
Strain: ATCC 15382.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48935 Genomic DNA. Translation: AAA88910.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW1X-ray2.70A/B/D/E/G/H/J/K1-256[»]
1AW2X-ray2.65A/B/D/E/G/H/J/K1-256[»]
ProteinModelPortalP50921.
SMRP50921. Positions 2-240.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00147_B. TIM_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR21139. Triophos_ismrse. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. Triophos_ismrse. 1 hit.
TIGRFAMsTIGR00419. Tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS_VIBMA
AccessionPrimary (citable) accession number: P50921
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 31, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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