Skip Header

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

Q1LTT4 (TPIS_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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

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:BCI_0169
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length256 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 – 256256Triosephosphate isomerase HAMAP MF_00147_B
PRO_0000307435

Sites

Active site961Electrophile By similarity
Active site1681Proton acceptor By similarity
Binding site91Substrate By similarity
Binding site111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LTT4 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 87C95FCA02A9DF38

FASTA25628,116
        10         20         30         40         50         60 
MRHPLVIGNW KLNGSKHMVS NFIISLRNQL SNMINCCNVA IAPPMIYLDR AKSYLTGSHI 

        70         80         90        100        110        120 
ALGAQNVDLH VSGAFTGEIS AKMLKDIGAK YIIIGHIERR LYHKESNEDI ANKFACLKNE 

       130        140        150        160        170        180 
GLIPVLCIGE TKEENEKDQT KAICVRQLDY ILNIVGTQAF KNAVIAYEPI WAIATGKSAN 

       190        200        210        220        230        240 
PLQIQKIHKF IRSYLFNHDQ AIAEQVIIQY GGSVNASNAA ELFNQPDVDG ALVGGASLKA 

       250 
DIFATIIKAA ARAKKN 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13817.1.
RefSeqYP_588630.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTT4.
SMRQ1LTT4. Positions 1-255.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056146.
GenomeReviewsGene locus BCI_0169 in contig CP000238_GR.
KEGGbci:BCI_0169.
PATRIC21073833. VBIBauCic75062_0161.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0149.
HOGENOMHBG708281.
OMAIEKNGTM.
PhylomeDBQ1LTT4.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0169-MONOMER.

Family and domain databases

HAMAPMF_00147_B. TIM_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
[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. False negative.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS_BAUCH
AccessionPrimary (citable) accession number: Q1LTT4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 37 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