ID Q2KWK3_BORA1 Unreviewed; 249 AA.
AC Q2KWK3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 51.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=tpiA; OrderedLocusNames=BAV2659;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA Squares S., Woodward J., Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella
RT avium with those of B. bronchiseptica, B. pertussis, and B.
RT parapertussis reveals extensive diversity in surface structures
RT associated with host interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC phosphate.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
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DR EMBL; AM167904; CAJ50269.1; -; Genomic_DNA.
DR RefSeq; YP_787157.1; NC_010645.1.
DR ProteinModelPortal; Q2KWK3; -.
DR STRING; 360910.BAV2659; -.
DR GeneID; 6267750; -.
DR KEGG; bav:BAV2659; -.
DR PATRIC; 21131593; VBIBorAvi43433_2689.
DR eggNOG; COG0149; -.
DR HOGENOM; HOG000226413; -.
DR KO; K01803; -.
DR OMA; ANTVIAY; -.
DR ProtClustDB; PRK00042; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:HAMAP.
DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; Triophos_ismrse; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Pentose shunt.
FT ACT_SITE 100 100 Electrophile (By similarity).
FT ACT_SITE 171 171 Proton acceptor (By similarity).
FT BINDING 15 15 Substrate (By similarity).
FT BINDING 17 17 Substrate (By similarity).
SQ SEQUENCE 249 AA; 25554 MW; 7B2E52E0281A0418 CRC64;
MTETANRRSR LVLGNWKMHG SLAENASLLA ALRAADPALH CEIGVCVPFP YLAQASAALS
GSAISWGAQD VSAQAKGAFT GEVSASMLKD FGSRWALAGH SERRTLHGET DQEVADKARA
ALAAGLRPVV CVGESLAERE AGQTLAIIER QLAPVLALGR EAVAGMVLAY EPVWAIGTGL
SATPEQAQEV HAAIRAALAG LGATQVQVLY GGSVKAANAA SLFAMADIDG ALVGGASLVA
EEFLRIAAN
//
