ID TPIS_ACIB3 Reviewed; 264 AA.
AC B7H1F6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=tpiA; OrderedLocusNames=ABBFA_003206;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter;
OC Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/JB.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H.,
RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A.,
RA Hujer A.M., Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant
RT Acinetobacter baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001172; ACJ57351.1; -; Genomic_DNA.
DR RefSeq; YP_002327087.1; NC_011595.1.
DR STRING; 557600.ABBFA_003206; -.
DR EnsemblBacteria; ACJ57351; ACJ57351; ABBFA_003206.
DR GeneID; 7057810; -.
DR KEGG; abb:ABBFA_003206; -.
DR PATRIC; 20707873; VBIAciBau42682_3095.
DR eggNOG; COG0149; -.
DR HOGENOM; HOG000226413; -.
DR KO; K01803; -.
DR OMA; QEVCGAI; -.
DR ProtClustDB; PRK00042; -.
DR BioCyc; ABAU557600:GH0U-1361-MONOMER; -.
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 CHAIN 1 264 Triosephosphate isomerase.
FT /FTId=PRO_1000117991.
FT ACT_SITE 106 106 Electrophile (By similarity).
FT ACT_SITE 179 179 Proton acceptor (By similarity).
FT BINDING 13 13 Substrate (By similarity).
FT BINDING 15 15 Substrate (By similarity).
SQ SEQUENCE 264 AA; 28217 MW; 9982884929BE714F CRC64;
MSGSTITPWV VGNWKMNPMR ANANQLIEEF KQLLQQNQIA DENCHVGVAP VSIALTTVQA
QLQDAARTVY TVAQDVSRVA GTGAYTGEVS AELLKDSQIN FVLVGHSERR DIFGDNVEIL
KAKLQNALNA GMTVIYCVGE SLEQREQGQA EQVVLQQICD IAPVVTAEQW QNQVVIAYEP
IWAIGTGKTA SPQDAQAMHA KIREGLCQLT SAGSNIAILY GGSVKAENAV ELAACPDING
ALVGGASLNA ASFYQIVQAF AQSK
//
