P35144 (TPIS_BACMD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Triosephosphate isomerase
Short name=TIM
EC=5.3.1.1

Alternative name(s):
Triose-phosphate isomerase

Gene names

Name:	tpiA
Synonyms:	tpi
Ordered Locus Names:	BMD_5036

Organism

Bacillus megaterium (strain DSM 319) [Complete proteome] [HAMAP]

Taxonomic identifier

592022 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
Subcellular location	Cytoplasm By similarity HAMAP MF_00147_B.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Cellular component	Cytoplasm
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gluconeogenesis 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 component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	triose-phosphate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 251	251	Triosephosphate isomerase HAMAP MF_00147_B		PRO_0000090177
Sites
	Active site	95	1	Electrophile By similarity
	Active site	167	1	Proton acceptor By similarity
	Binding site	9	1	Substrate By similarity
	Binding site	11	1	Substrate By similarity
Amino acid modifications
	Modified residue	213	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35144 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: D1190430EC72357D	FASTA	251	26,921
	10 20 30 40 50 60 MRKPIIAGNW KMNKVLSEAT SFVEEVKGAV PSPESVDSVV CAPALFLDRL VEATKGTDLK 70 80 90 100 110 120 IGAQNMHFEE NGAFTGEVSP VALADLGVNY VILGHSERRE MFAETDETVN QKTIAAFKHG 130 140 150 160 170 180 LTPIVCCGET NEEYEQDQTK TVVANQVQKA LAGLTDEQVK QTVIAYEPIW AIGTGKSSTA 190 200 210 220 230 240 EGANEVCAYI RSVVAEQFSQ DVADAVRIQY GGSVKPANIK EYMSQSDIDG ALVGGASLEA 250 DSFLQLLEAG K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus." Schlaepfer B.S., Zuber H. Gene 122:53-62(1992) [PubMed: 1452037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure." Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S. Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 319.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M87647 Genomic DNA. Translation: AAA73204.1. M87648 Genomic DNA. Translation: AAA73207.1. CP001982 Genomic DNA. Translation: ADF41836.1.
PIR	JQ1955.
RefSeq	YP_003600186.1. NC_014103.1.
3D structure databases
ProteinModelPortal	P35144.
SMR	P35144. Positions 2-251.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000420587; EBBACP00000418454; EBBACG00000422351.
GeneID	9120427.
GenomeReviews	Gene locus BMD_5036 in contig CP001982_GR.
KEGG	bmd:BMD_5036.
PATRIC	37260259. VBIBacMeg104484_5014.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000002739.
ProtClustDB	CLSK2840959.
Enzyme and pathway databases
BRENDA	5.3.1.1. 672.
Family and domain databases
HAMAP	MF_00147_B. TIM_B. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR022896. TrioseP_Isoase_bac/euk. IPR000652. Triosephosphate_isomerase. IPR020861. Triosephosphate_isomerase_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01803.
PANTHER	PTHR21139. Triophos_ismrse. 1 hit.
Pfam	PF00121. TIM. 1 hit. [Graphical view]
SUPFAM	SSF51351. Triophos_ismrse. 1 hit.
TIGRFAMs	TIGR00419. Tim. 1 hit.
PROSITE	PS00171. TIM_1. 1 hit. PS51440. TIM_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TPIS_BACMD

Accession

Primary (citable) accession number: P35144
Secondary accession number(s): D5DNA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program