TPIS_ECODH
ID TPIS_ECODH Reviewed; 255 AA.
AC B1XB85;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:23695562};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:23695562};
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=ECDH10B_4108;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP AND SUBUNIT.
RX PubMed=23695562; DOI=10.1107/s1744309113010841;
RA Kozlov G., Vinaik R., Gehring K.;
RT "Triosephosphate isomerase is a common crystallization contaminant of
RT soluble His-tagged proteins produced in Escherichia coli.";
RL Acta Crystallogr. F 69:499-502(2013).
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 ECO:0000269|PubMed:23695562}.
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; CP000948; ACB04931.1; -; Genomic_DNA.
DR RefSeq; WP_001216325.1; NC_010473.1.
DR PDB; 4IOT; X-ray; 1.85 A; A/B=1-255.
DR PDBsum; 4IOT; -.
DR AlphaFoldDB; B1XB85; -.
DR SMR; B1XB85; -.
DR GeneID; 66672173; -.
DR KEGG; ecd:ECDH10B_4108; -.
DR HOGENOM; CLU_024251_2_1_6; -.
DR OMA; QEVCGAI; -.
DR BioCyc; ECOL316385:ECDH10B_RS20920-MON; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..255
FT /note="Triosephosphate isomerase"
FT /id="PRO_1000096495"
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 ECO:0000269|PubMed:23695562"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:23695562"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 180..195
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4IOT"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:4IOT"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4IOT"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:4IOT"
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
