Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1TLL4 (TPIS_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
Ordered Locus Names:Aave_1261
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00147_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00147_B.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
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 – 251251Triosephosphate isomerase HAMAP MF_00147_B
PRO_0000307418

Sites

Active site981Electrophile By similarity
Active site1691Proton acceptor By similarity
Binding site101Substrate By similarity
Binding site121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TLL4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6F96A8F4C7DEA390

FASTA25126,039
        10         20         30         40         50         60 
MTKKKLIAGN WKMNGTLGAN AALLQALRGG LEAGAYQNVD VAVAVPAAYL AQVQGLVEGS 

        70         80         90        100        110        120 
AIALAAQDVS RHEAGAYTGE VSAAMLQEFG VRYVLVGHSE RRQYHGETDE QVAEKAQRAL 

       130        140        150        160        170        180 
AAGITPVVCV GETLAEREAG QTEAVVKRQL AAVIHLNGHC ISETVVAYEP VWAIGTGRTA 

       190        200        210        220        230        240 
TPEQAQQVHA VLRAQLAAAS EHADRIRLLY GGSMNAANAA ALLAQPDIDG GLVGGASLKA 

       250 
QDFLQIIAAA A

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000512 Genomic DNA. Translation: ABM31852.1.
RefSeqYP_969626.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TLL4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TLL4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4668329.
GenomeReviewsGene locus Aave_1261 in contig CP000512_GR.
KEGGaav:Aave_1261.
NMPDRfig|397945.5.peg.1106.
PATRIC20677576. VBIAciCit38535_1292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0149.
HOGENOMHBG708281.
OMAANTVIAY.
PhylomeDBA1TLL4.
ProtClustDBPRK00042.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_1261-MONOMER.

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.
KOK01803.
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_ACIAC
AccessionPrimary (citable) accession number: A1TLL4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 35 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents