C7C913 (C7C913_METED) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Triosephosphate isomerase HAMAP-Rule MF_00147
Short name=TIM HAMAP-Rule MF_00147
EC=5.3.1.1 HAMAP-Rule MF_00147

Alternative name(s):
Triose-phosphate isomerase HAMAP-Rule MF_00147

Gene names

Name:	tpiA HAMAP-Rule MF_00147 EMBL CAX27320.1
Ordered Locus Names:	METDI5716 EMBL CAX27320.1

Organism

Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium dichloromethanicum (strain DM4)) [Complete proteome] [HAMAP] EMBL CAX27320.1

Taxonomic identifier

661410 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium › Methylobacterium extorquens group › Methylobacterium extorquens

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate. RuleBase RU000517 SAAS SAAS020861 HAMAP-Rule MF_00147
Pathway	Carbohydrate biosynthesis; gluconeogenesis. RuleBase RU000517 SAAS SAAS020861 HAMAP-Rule MF_00147 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. RuleBase RU000517 SAAS SAAS020861 HAMAP-Rule MF_00147
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00147 SAAS SAAS020861
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00147.
Sequence similarities	Belongs to the triosephosphate isomerase family. HAMAP-Rule MF_00147

Ontologies

Keywords
Biological process	Gluconeogenesis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Glycolysis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Pentose shunt RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147
Cellular component	Cytoplasm HAMAP-Rule MF_00147
Molecular function	Isomerase RuleBase RU000517 SAAS SAAS020861 HAMAP-Rule MF_00147 EMBL CAX27320.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: HAMAP glycolysis Inferred from electronic annotation. Source: HAMAP pentose-phosphate shunt Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	triose-phosphate isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	100	1	Electrophile By similarity HAMAP-Rule MF_00147
	Active site	170	1	Proton acceptor By similarity HAMAP-Rule MF_00147
	Binding site	13	1	Substrate By similarity HAMAP-Rule MF_00147
	Binding site	15	1	Substrate By similarity HAMAP-Rule MF_00147

Sequences

	Sequence		Length	Mass (Da)
	C7C913 [UniParc]. Last modified September 22, 2009. Version 1. Checksum: 0F35FB416B7D4E0E	FASTA	254	26,563
	10 20 30 40 50 60 MASEGRRPLV AGNWKMNGLL SSVPTVEAIR DGLSPALADK IDVLICPPAT LISSCVAAVY 70 80 90 100 110 120 GSVVAIGGQN LHARPSGAFT GSISAEMFAD LGATYVIVGH SERRAYHYET DDGVHAKALG 130 140 150 160 170 180 ARRAGLRGII CVGETMEERQ QGRALDIVRA QLAIGLPKGA TGADTVIAYE PVWAIGSGRT 190 200 210 220 230 240 PTATEIAEVH ASLREMLDKL VGEEAHKIRI LYGGSVKPSN ARELMAVENV DGALVGGASL 250 VAEDFLGICR AYEG

References

[1]

"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources." Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E. PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 5838 / DM4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FP103042 Genomic DNA. Translation: CAX27320.1.
RefSeq	YP_003071125.1. NC_012988.1.
3D structure databases
ProteinModelPortal	C7C913.
ModBase	Search...
Protein-protein interaction databases
STRING	661410.METDI5716.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAX27320; CAX27320; METDI5716.
GeneID	8194883.
KEGG	mdi:METDI5716.
PATRIC	22529885. VBIMetExt143287_5445.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0149.
HOGENOM	HOG000226414.
KO	K01803.
OMA	QEVCGAI.
ProtClustDB	PRK00042.
Enzyme and pathway databases
BioCyc	MEXT661410:GJA1-5625-MONOMER.
UniPathway	UPA00109; UER00189. UPA00138.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00147_B. TIM_B.
InterPro	IPR013785. Aldolase_TIM. IPR022896. TrioseP_Isoase_bac/euk. IPR000652. Triosephosphate_isomerase. IPR020861. Triosephosphate_isomerase_AS. [Graphical view]
PANTHER	PTHR21139. PTHR21139. 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

C7C913_METED

Accession

Primary (citable) accession number: C7C913

Entry history

Integrated into UniProtKB/TrEMBL:	September 22, 2009
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)