TPIS_ACTP2
ID TPIS_ACTP2 Reviewed; 256 AA.
AC A3N3L9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=APL_1925;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN75005.1; -; Genomic_DNA.
DR RefSeq; WP_005599672.1; NC_009053.1.
DR AlphaFoldDB; A3N3L9; -.
DR SMR; A3N3L9; -.
DR STRING; 416269.APL_1925; -.
DR EnsemblBacteria; ABN75005; ABN75005; APL_1925.
DR GeneID; 66258720; -.
DR KEGG; apl:APL_1925; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_1_6; -.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001432; 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 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;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..256
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000307420"
FT ACT_SITE 97
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
SQ SEQUENCE 256 AA; 26522 MW; 273D2543F1588216 CRC64;
MARRPLVMGN WKLNGSKAFT KELIAGLKAE LADVKGCDVA IAPPVMYLAE AEAALAGQSV
IALGAQNVDV NVQGAFTGDI STEMLKDFGA KYIIIGHSER RTYHKECDTF IAKKFAALKA
AGLVPVLCIG ETEAENEAGQ TEAVCAKQID AVIDALGVEA FNGAVIAYEP IWAIGTGKSA
TPAQAQAVHA FIRGHIAAKS QAVADQVIIQ YGGSVNDANA AELFTQPDID GALVGGASLK
APAFAVIVKA AEKAKA