TPIS_ECOLI
ID TPIS_ECOLI Reviewed; 255 AA.
AC P0A858; P04790; Q2M8L5;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:6092857};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:15299515};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:6092857};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:6092857, ECO:0000269|PubMed:9442062};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:6092857};
GN Synonyms=tpi; OrderedLocusNames=b3919, JW3890;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX PubMed=6092857; DOI=10.1007/bf00332765;
RA Pichersky E., Gottlieb L.D., Hess J.F.;
RT "Nucleotide sequence of the triose phosphate isomerase gene of Escherichia
RT coli.";
RL Mol. Gen. Genet. 195:314-320(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-9.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 1-14.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12;
RX PubMed=17895580; DOI=10.1266/ggs.82.291;
RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL Genes Genet. Syst. 82:291-299(2007).
RN [8]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [9]
RP INDUCTION.
RX PubMed=7493933; DOI=10.1074/jbc.270.49.29096;
RA Sabnis N.A., Yang H., Romeo T.;
RT "Pleiotropic regulation of central carbohydrate metabolism in Escherichia
RT coli via the gene csrA.";
RL J. Biol. Chem. 270:29096-29104(1995).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9442062; DOI=10.1074/jbc.273.4.2199;
RA Alvarez M., Zeelen J.P., Mainfroid V., Rentier-Delrue F., Martial J.A.,
RA Wyns L., Wierenga R.K., Maes D.;
RT "Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio
RT marinus. Kinetic and structural properties.";
RL J. Biol. Chem. 273:2199-2206(1998).
RN [11]
RP INDUCTION.
RC STRAIN=K12 / W3110;
RX PubMed=16223443; DOI=10.1186/1471-2180-5-59;
RA Yohannes E., Thurber A.E., Wilks J.C., Tate D.P., Slonczewski J.L.;
RT "Polyamine stress at high pH in Escherichia coli K-12.";
RL BMC Microbiol. 5:59-59(2005).
RN [12]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=24745552; DOI=10.1186/1475-2859-13-58;
RA Velur Selvamani R.S., Telaar M., Friehs K., Flaschel E.;
RT "Antibiotic-free segregational plasmid stabilization in Escherichia coli
RT owing to the knockout of triosephosphate isomerase (tpiA).";
RL Microb. Cell Fact. 13:58-58(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=8309937; DOI=10.1093/protein/6.8.893;
RA Mainfroid V., Goraj K., Rentier-Delrue F., Houbrechts A., Loiseau A.,
RA Gohimont A.-C., Noble M.E.M., Borchert T.V., Wierenga R.K., Martial J.A.;
RT "Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue
RT leads to a stable and active hybrid enzyme.";
RL Protein Eng. 6:893-900(1993).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=15299515; DOI=10.1107/s0907444993002628;
RA Noble M.E.M., Zeelen J.P., Wierenga R.K., Mainfroid V., Goraj K.,
RA Gohimont A.-C., Martial J.A.;
RT "Structure of triosephosphate isomerase from Escherichia coli determined at
RT 2.6-A resolution.";
RL Acta Crystallogr. D 49:403-417(1993).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=7809033; DOI=10.1093/protein/7.8.945;
RA Kishan R., Zeelen J.P., Noble M.E., Borchert T.V., Mainfroid V., Goraj K.,
RA Martial J.A., Wierenga R.K.;
RT "Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a
RT chimeric E. coli TIM having the eighth beta alpha-unit replaced by the
RT equivalent unit of chicken TIM.";
RL Protein Eng. 7:945-951(1994).
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 ECO:0000269|PubMed:9442062}.
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 ECO:0000269|PubMed:6092857, ECO:0000269|PubMed:9442062};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1030 uM for D-glyceraldehyde 3-phosphate (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9442062};
CC Note=kcat is 54000 min(-1) for isomerase activity with D-
CC glyceraldehyde 3-phosphate as substrate (at 25 degrees Celsius).
CC {ECO:0000269|PubMed:9442062};
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 ECO:0000269|PubMed:15299515, ECO:0000269|PubMed:7809033,
CC ECO:0000269|PubMed:8309937}.
CC -!- INTERACTION:
CC P0A858; P29745: pepT; NbExp=7; IntAct=EBI-368978, EBI-555639;
CC P0A858; P09373: pflB; NbExp=7; IntAct=EBI-368978, EBI-546682;
CC P0A858; P0A858: tpiA; NbExp=3; IntAct=EBI-368978, EBI-368978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147,
CC ECO:0000305}.
CC -!- INDUCTION: Induced by CsrA and repressed by spermidine.
CC {ECO:0000269|PubMed:16223443, ECO:0000269|PubMed:7493933}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulates methylglyoxal
CC and are unable to grow on glucose, lactate or other carbon sources.
CC {ECO:0000269|PubMed:24745552}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X00617; CAA25253.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03051.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76901.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77391.1; -; Genomic_DNA.
DR PIR; B65198; ISECT.
DR RefSeq; NP_418354.1; NC_000913.3.
DR RefSeq; WP_001216325.1; NZ_STEB01000017.1.
DR PDB; 1TMH; X-ray; 2.80 A; A/B/C/D=1-255.
DR PDB; 1TRE; X-ray; 2.60 A; A/B=1-255.
DR PDBsum; 1TMH; -.
DR PDBsum; 1TRE; -.
DR AlphaFoldDB; P0A858; -.
DR SMR; P0A858; -.
DR BioGRID; 4262647; 12.
DR BioGRID; 852706; 2.
DR DIP; DIP-31849N; -.
DR IntAct; P0A858; 28.
DR STRING; 511145.b3919; -.
DR SWISS-2DPAGE; P0A858; -.
DR jPOST; P0A858; -.
DR PaxDb; P0A858; -.
DR PRIDE; P0A858; -.
DR EnsemblBacteria; AAC76901; AAC76901; b3919.
DR EnsemblBacteria; BAE77391; BAE77391; BAE77391.
DR GeneID; 66672173; -.
DR GeneID; 948409; -.
DR KEGG; ecj:JW3890; -.
DR KEGG; eco:b3919; -.
DR PATRIC; fig|1411691.4.peg.2786; -.
DR EchoBASE; EB1008; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_1_6; -.
DR InParanoid; P0A858; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; P0A858; -.
DR BioCyc; EcoCyc:TPI-MON; -.
DR BioCyc; MetaCyc:TPI-MON; -.
DR BRENDA; 5.3.1.1; 2026.
DR SABIO-RK; P0A858; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P0A858; -.
DR PRO; PR:P0A858; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IMP:EcoliWiki.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..255
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090217"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT CONFLICT 67
FT /note="D -> N (in Ref. 1; CAA25253)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1TRE"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 180..204
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1TRE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1TRE"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1TMH"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1TRE"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:1TRE"
SQ SEQUENCE 255 AA; 26972 MW; E398251020012D94 CRC64;
MRHPLVMGNW KLNGSRHMVH ELVSNLRKEL AGVAGCAVAI APPEMYIDMA KREAEGSHIM
LGAQNVDLNL SGAFTGETSA AMLKDIGAQY IIIGHSERRT YHKESDELIA KKFAVLKEQG
LTPVLCIGET EAENEAGKTE EVCARQIDAV LKTQGAAAFE GAVIAYEPVW AIGTGKSATP
AQAQAVHKFI RDHIAKVDAN IAEQVIIQYG GSVNASNAAE LFAQPDIDGA LVGGASLKAD
AFAVIVKAAE AAKQA
