TPIS_CLOPE
ID TPIS_CLOPE Reviewed; 248 AA.
AC Q8XKU1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:26206330};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:26206330};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:26206330};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=CPE1302;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=13 / Type A;
RX PubMed=26206330; DOI=10.1039/c5cp01599e;
RA Romero-Romero S., Costas M., Rodriguez-Romero A.,
RA Alejandro Fernandez-Velasco D.;
RT "Reversibility and two state behaviour in the thermal unfolding of
RT oligomeric TIM barrel proteins.";
RL Phys. Chem. Chem. Phys. 17:20699-20714(2015).
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:26206330}.
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:26206330};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.72 mM for G3P {ECO:0000269|PubMed:26206330};
CC Note=kcat is 6348 sec(-1) for isomerase activity.
CC {ECO:0000269|PubMed:26206330};
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:26206330}.
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; BA000016; BAB81008.1; -; Genomic_DNA.
DR RefSeq; WP_003450470.1; NC_003366.1.
DR PDB; 4Y8F; X-ray; 1.54 A; A=1-248.
DR PDBsum; 4Y8F; -.
DR AlphaFoldDB; Q8XKU1; -.
DR SMR; Q8XKU1; -.
DR STRING; 195102.gene:10490565; -.
DR EnsemblBacteria; BAB81008; BAB81008; BAB81008.
DR GeneID; 29571381; -.
DR KEGG; cpe:CPE1302; -.
DR HOGENOM; CLU_024251_2_3_9; -.
DR OMA; QEVCGAI; -.
DR SABIO-RK; Q8XKU1; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000818; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090211"
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 166
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 172
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 STRAND 5..9
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4Y8F"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:4Y8F"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 179..197
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4Y8F"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:4Y8F"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4Y8F"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:4Y8F"
SQ SEQUENCE 248 AA; 27058 MW; 8503792DED4B573A CRC64;
MRTPIIAGNW KMHYTIDEAV KLVEELKPLV KDAKCEVVVC PTFVCLDAVK KAVEGTNIKV
GAQNMHFEEK GAFTGEIAPR MLEAMNIDYV IIGHSERREY FNETDETCNK KVKAAFAHNL
TPILCCGETL EQRENGTTND VIKAQITADL EGLTKEQAEK VVIAYEPIWA IGTGKTATSD
QANETIAAIR AMVAEMFGQE VADKVRIQYG GSVKPNTIAE QMAKSDIDGA LVGGASLVAA
DFAQIVNY
