Q2SZN7 (Q2SZN7_BURTA) 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
Ordered Locus Names:	BTH_I1058

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP] EMBL ABC37425.1

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia thailandensis

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate. SAAS SAAS020861 HAMAP-Rule MF_00147
Pathway	Carbohydrate biosynthesis; gluconeogenesis. SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517
Subunit structure	Homodimer By similarity. SAAS SAAS020861 HAMAP-Rule MF_00147
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00147.
Sequence similarities	Belongs to the triosephosphate isomerase family. HAMAP-Rule MF_00147 RuleBase RU004162

Ontologies

Keywords
Biological process	Gluconeogenesis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Glycolysis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Pentose shunt SAAS SAAS020861 RuleBase RU003527 HAMAP-Rule MF_00147
Cellular component	Cytoplasm HAMAP-Rule MF_00147
Molecular function	Isomerase SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517 EMBL ABC37425.1
Technical term	3D-structure PDB 4G1K 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	99	1	Electrophile By similarity HAMAP-Rule MF_00147
	Active site	171	1	Proton acceptor By similarity HAMAP-Rule MF_00147
	Binding site	12	1	Substrate By similarity HAMAP-Rule MF_00147
	Binding site	14	1	Substrate By similarity HAMAP-Rule MF_00147

Sequences

	Sequence		Length	Mass (Da)
	Q2SZN7 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 9EAA6BF0A7118B9C	FASTA	251	25,940
	10 20 30 40 50 60 MSKQRIKRVI GNWKMHGRLS GNQALLTEVA QGAQAVHDNV AIGVCVPFPY LAQAQAQLQG 70 80 90 100 110 120 GRVSWGSQDV SAHEQGAYTG EVAAGMVAEF GAAYAIVGHS ERRAYHGESN ETVAAKARRA 130 140 150 160 170 180 LAAGLTPIVC VGETLAEREA GTTEQVVGAQ LDAVLAVLSP DEAARIVVAY EPVWAIGTGK 190 200 210 220 230 240 SATAEQAQQV HAFLRGRLAA KGAGHVSLLY GGSVKADNAA ELFGQPDIDG GLIGGASLKS 250 GDFLAICRAA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies." Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D. BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.
[2]	"Crystal structure of triosephosphate isomerase from Burkholderia thailandensis." Seattle Structural Genomics Center for Infectious Disease (SSGCID) Edwards T.E., Fairman J.W. Submitted (JUL-2012) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000086 Genomic DNA. Translation: ABC37425.1.

RefSeq

YP_441612.1. NC_007651.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4G1K	X-ray	2.35	A/B/C/D	1-251	[»]

ProteinModelPortal

Q2SZN7.

ModBase

Search...

Protein-protein interaction databases

STRING

271848.BTH_I1058.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABC37425; ABC37425; BTH_I1058.

GeneID

3848210.

KEGG

bte:BTH_I1058.

PATRIC

19305006. VBIBurTha36512_3819.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0149.

HOGENOM

HOG000226413.

KO

K01803.

OMA

ANTVIAY.

ProtClustDB

PRK00042.

Enzyme and pathway databases

BioCyc

BTHA271848:GJMY-1058-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

Q2SZN7_BURTA

Accession

Primary (citable) accession number: Q2SZN7

Entry history

Integrated into UniProtKB/TrEMBL:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)