(data stored in ACNUC29543 zone)

SWISSPROT: TPIS_ACIBT

ID   TPIS_ACIBT              Reviewed;         264 AA.
AC   A3M1K0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=A1S_0330;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00147};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
DR   EMBL; CP000521; ABO10794.2; -; Genomic_DNA.
DR   SMR; A3M1K0; -.
DR   EnsemblBacteria; ABO10794; ABO10794; A1S_0330.
DR   KEGG; acb:A1S_0330; -.
DR   HOGENOM; HOG000226413; -.
DR   KO; K01803; -.
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:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
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; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M1K0.
DR   SWISS-2DPAGE; A3M1K0.
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    264       Triosephosphate isomerase.
FT                                /FTId=PRO_1000096469.
FT   REGION       13     15       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      244    245       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    106    106       Electrophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    179    179       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   BINDING     185    185       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00147}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
SQ   SEQUENCE   264 AA;  28227 MW;  6A81884929BC3A22 CRC64;
     MSGSTITPWV VGNWKMNPMR ANANQLIEEF KQLLQQNQIA DENCHVGVAP VSIALTTVQA
     QLQDAARTVY TVAQDVSRVA GTGAYTGEVS AELLKDSQIN FVLVGHSERR DIFGDNVEIL
     KAKLQNALNA GMTVIYCVGE SLEQREQGQA EQVVLQQICD IAPVVTAEQW QNQVVIAYEP
     IWAIGTGKTA SPQDAQAMHA KIREGLCQLT PAGSNIAILY GGSVKAENAV ELAACPDING
     ALVGGASLNA ASFYQIVQAF AQSK
//

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