TPIS_MYCPI
ID TPIS_MYCPI Reviewed; 150 AA.
AC P47721;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
DE Flags: Fragment;
GN Name=tpiA; Synonyms=tim, tpi;
OS Mycoplasma pirum (Mycoplasmoides pirum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=2122;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BER;
RX PubMed=8349569; DOI=10.1128/jb.175.16.5281-5285.1993;
RA Tham T.N., Ferris S., Kovacic R., Montagnier L., Blanchard A.;
RT "Identification of Mycoplasma pirum genes involved in the salvage pathways
RT for nucleosides.";
RL J. Bacteriol. 175:5281-5285(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC ProRule:PRU10127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|PROSITE-ProRule:PRU10127}.
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DR EMBL; L13289; AAA25435.1; -; Genomic_DNA.
DR PIR; F53312; F53312.
DR AlphaFoldDB; P47721; -.
DR SMR; P47721; -.
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-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..>150
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090253"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT NON_TER 150
SQ SEQUENCE 150 AA; 17040 MW; 898DB1968EB30487 CRC64;
MKKRIIIGNW KTNKTQKEVK EFFKILNASL KNKNICCTFG VAPVAIHLEL AKSLAPKQMI
IAAQDANYIS SGAFTGTISW SQLKDIKIKY VIVGHSERRM YYNETDDIVN KKVKNLLENK
MIPILCIGGN IEEFNNKKTY QVCATQLKKA