Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q986N6 (TPIS2_RHILO)

Last modified February 9, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Triosephosphate isomerase 2
      Short name=TIM 2
    EC=5.3.1.1
Alternative name(s):
    Triose-phosphate isomerase 2
Gene names
Name: tpiA2
Ordered Locus Names: mlr7275
OrganismRhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier381 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147

Subunit structure

Homodimer By similarity. HAMAP MF_00147

Subcellular location

Cytoplasm Probable HAMAP MF_00147.

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: HAMAP

glycolysis

Inferred from electronic annotation. Source: HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Triosephosphate isomerase 2 HAMAP MF_00147
PRO_0000090275

Sites

Active site971Electrophile By similarity
Active site1701Proton acceptor By similarity
Binding site121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q986N6-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 336F73D7EB87F653

FASTA25427,199
        10         20         30         40         50         60 
MRVVYWVGTS WKMNKTLAEA LDFAERLAGF IPGFDDRIQP FVIPPFTAVR EVKRALSSTR 

        70         80         90        100        110        120 
IKVGAQNMHW ADAGAWTGEI SPPMLRDCGL DLVELGHSER REHFGETDRT VGLKTAAAVK 

       130        140        150        160        170        180 
HGMIPLICVG ETLAERESGQ ADAVLSAQVE GALQFLEGEA KTAKILFAYE PVWAIGDKGI 

       190        200        210        220        230        240 
PASADYADKQ QALIKTVAGA LLPSVPPVLY GGSVNPGNAA ELVGQPNIDG LFIGRSAWQA 

       250 
DGYIDILGRA SAAI 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB53417.1.
RefSeqNP_107631.1.

3D structure databases

SMRQ986N6. Positions 5-250.
ModBaseSearch...

Genome annotation databases

GeneID1230286.
GenomeReviewsGene locus mlr7275 in contig BA000012_GR.
KEGGmlo:mlr7275.
NMPDRfig|266835.1.peg.5732.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG708281.
OMAEHFGETD.

Enzyme and pathway databases

BRENDA5.3.1.1. 3315.

Family and domain databases

HAMAPMF_00147_B. TIM_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
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]
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS2_RHILO
AccessionPrimary (citable) accession number: Q986N6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2001
Last modified: February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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