TPIS_HELPY
ID TPIS_HELPY Reviewed; 234 AA.
AC P56076;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17957775};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17957775};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17957775};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17957775};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; Synonyms=tpi;
GN OrderedLocusNames=HP_0194;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-234 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF LYS-183 AND ASP-213, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=17957775; DOI=10.1002/prot.21709;
RA Chu C.H., Lai Y.J., Huang H., Sun Y.J.;
RT "Kinetic and structural properties of triosephosphate isomerase from
RT Helicobacter pylori.";
RL Proteins 71:396-406(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 ECO:0000269|PubMed:17957775}.
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:17957775};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.46 uM for D-glyceraldehyde 3-phosphate (at pH 7.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:17957775};
CC Note=kcat is 88000 min(-1) for isomerase activity with D-
CC glyceraldehyde 3-phosphate as substrate (at pH 7.5 and 25 degrees
CC Celsius). {ECO:0000269|PubMed:17957775};
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:17957775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- MASS SPECTROMETRY: Mass=28108; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17957775};
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR EMBL; AE000511; AAD07261.1; -; Genomic_DNA.
DR PIR; B64544; B64544.
DR RefSeq; NP_206993.1; NC_000915.1.
DR RefSeq; WP_000160988.1; NC_018939.1.
DR PDB; 2JGQ; X-ray; 2.30 A; A/B=2-234.
DR PDBsum; 2JGQ; -.
DR AlphaFoldDB; P56076; -.
DR SMR; P56076; -.
DR DIP; DIP-3273N; -.
DR IntAct; P56076; 5.
DR MINT; P56076; -.
DR STRING; 85962.C694_00965; -.
DR PaxDb; P56076; -.
DR EnsemblBacteria; AAD07261; AAD07261; HP_0194.
DR KEGG; hpy:HP_0194; -.
DR PATRIC; fig|85962.47.peg.209; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; QEVCGAI; -.
DR PhylomeDB; P56076; -.
DR BRENDA; 5.3.1.1; 2604.
DR SABIO-RK; P56076; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P56076; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
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; IBA:GO_Central.
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 PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1..234
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090228"
FT ACT_SITE 90
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:17957775"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:17957775"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:17957775"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:17957775"
FT MUTAGEN 183
FT /note="K->A: 3-fold decrease of the affinity and slight
FT decrease of the catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17957775"
FT MUTAGEN 183
FT /note="K->S: The affinity and the catalytic efficiency are
FT comparable to the wild-type."
FT /evidence="ECO:0000269|PubMed:17957775"
FT MUTAGEN 213
FT /note="D->A: The affinity and the catalytic efficiency are
FT comparable to the wild-type."
FT /evidence="ECO:0000269|PubMed:17957775"
FT MUTAGEN 213
FT /note="D->Q: The affinity and the catalytic efficiency are
FT comparable to the wild-type."
FT /evidence="ECO:0000269|PubMed:17957775"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2JGQ"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2JGQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2JGQ"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:2JGQ"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2JGQ"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:2JGQ"
SQ SEQUENCE 234 AA; 26708 MW; AFEB4FF92D5BC4D3 CRC64;
MTKIAMANFK SAMPIFKSHA YLKELEKTLK PQHFDRVFVF PDFFGLLPNS FLHFTLGVQN
AYPRDCGAFT GEITSKHLEE LKIHTLLIGH SERRTLLKES PSFLKEKFDF FKSKNFKIVY
CIGEELTTRE KGFKAVKEFL SEQLENIDLN YPNLVVAYEP IWAIGTKKSA SLEDIYLTHG
FLKQILNQKT PLLYGGSVNT QNAKEILGID SVDGLLIGSA SWELENFKTI ISFL
