TPIS_UREPA
ID TPIS_UREPA Reviewed; 238 AA.
AC Q9PQW2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=UU181;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.
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|HAMAP-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}.
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DR EMBL; AF222894; AAF30588.1; -; Genomic_DNA.
DR RefSeq; WP_006688831.1; NC_002162.1.
DR AlphaFoldDB; Q9PQW2; -.
DR SMR; Q9PQW2; -.
DR STRING; 273119.UU181; -.
DR EnsemblBacteria; AAF30588; AAF30588; UU181.
DR GeneID; 29672714; -.
DR KEGG; uur:UU181; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_3_14; -.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000423; Chromosome.
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 PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..238
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090311"
FT ACT_SITE 91
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ SEQUENCE 238 AA; 26978 MW; 4F804DEE27D52A8B CRC64;
MKYIIANFKM NATQELINHF LNNLTLFDEQ KIIIGLAPGD LYLKTFVNLA EIKKVNLYAQ
NPSLHNKGPY TGQISCLQLL DINIKNALVG HSEIRIDFSQ SIIDQKIKIS MDLLEQVIIC
VGETFDAYKQ NKSLNFVLNQ LANIINYKGL KKIIIAYEPI WAIGTDLELD FKHINYMIEG
IKTYLYNCTG INIPILYGGS VNDNNINELC NQKLIDGFLI GNASLDVNVF NKIIDKCK