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Q90XG0 (TPISB_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. 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 B

Short name=TIM-B
EC=5.3.1.1
Alternative name(s):
Triose-phosphate isomerase B
Gene names
Name:tpi1b
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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

   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

Initiator methionine11Removed By similarity
Chain2 – 248247Triosephosphate isomerase B
PRO_0000345141

Sites

Active site951Electrophile By similarity
Active site1651Proton acceptor By similarity
Binding site111Substrate By similarity
Binding site131Substrate By similarity

Experimental info

Sequence conflict561D → N in AAH53294. Ref.2
Sequence conflict561D → N in AAI52272. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q90XG0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CFD29D9A6E7918C8

FASTA24826,828
        10         20         30         40         50         60 
MSGRKFFVGG NWKMNGDKKS IEELANTLNS AKLNPDTEVV CGAPTIYLDY ARSKLDPNID 

        70         80         90        100        110        120 
VAAQNCYKVA KGAFTGEISP AMIKDCGVKW VILGHSERRH VFGESDELIG QKVAHALENG 

       130        140        150        160        170        180 
LGVIACIGEK LDEREAGITE KVVFAQTKFI ADNVKDWSKV VLAYEPVWAI GTGKTASPQQ 

       190        200        210        220        230        240 
AQEVHDKLRQ WLKTNVSEAV ANSVRIIYGG SVTGGTCKEL ASQKDLDGFL VGGASLKPEF 


IDIINAKA 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for a period of directional selection following gene duplication in a neurally expressed locus of triosephosphate isomerase."
Merritt T.J.S., Quattro J.M.
Genetics 159:689-697(2001) [PubMed: 11606544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF387819 mRNA. Translation: AAK85202.1.
BC152271 mRNA. Translation: AAI52272.1.
BC053294 mRNA. Translation: AAH53294.1.
IPIIPI00484161.
RefSeqNP_705954.2. NM_153668.4.
UniGeneDr.4157.

3D structure databases

HSSPHSSP built from PDB template 1TPH based on UniProtKB P00940.
ProteinModelPortalQ90XG0.
SMRQ90XG0. Positions 4-247.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ90XG0.

Proteomic databases

PRIDEQ90XG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000060056; ENSDARP00000060055; ENSDARG00000040988.
GeneID560753.
KEGGdre:560753.

Organism-specific databases

CTD560753.
ZFINZDB-GENE-020416-4. tpi1b.

Phylogenomic databases

eggNOGfiNOG12965.
GeneTreeENSGT00390000013354.
HOGENOMHBG708281.
HOVERGENHBG002599.
InParanoidQ90XG0.
OrthoDBEOG40S0GF.

Gene expression databases

ArrayExpressQ90XG0.
BgeeQ90XG0.

Family and domain databases

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 nameTPISB_DANRE
AccessionPrimary (citable) accession number: Q90XG0
Secondary accession number(s): Q7T315
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 1, 2001
Last modified: November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families