ID B9E6B3_CLOK1 Unreviewed; 248 AA.
AC B9E6B3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
DE Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN OrderedLocusNames=CKR_2987 {ECO:0000313|EMBL:BAH08038.1};
OS Clostridium kluyveri (strain NBRC 12016).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH08038.1, ECO:0000313|Proteomes:UP000007969};
RN [1] {ECO:0000313|Proteomes:UP000007969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA Yukawa H.;
RT "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT of Clostridia species.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC glyceraldehyde-3-phosphate (G3P). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00147,
CC ECO:0000256|RuleBase:RU363013};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00147, ECO:0000256|RuleBase:RU363013}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00147, ECO:0000256|RuleBase:RU363013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
CC ECO:0000256|RuleBase:RU363013}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000256|ARBA:ARBA00007422, ECO:0000256|HAMAP-Rule:MF_00147,
CC ECO:0000256|RuleBase:RU363013}.
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DR EMBL; AP009049; BAH08038.1; -; Genomic_DNA.
DR RefSeq; WP_012103713.1; NC_011837.1.
DR AlphaFoldDB; B9E6B3; -.
DR SMR; B9E6B3; -.
DR KEGG; ckr:CKR_2987; -.
DR HOGENOM; CLU_024251_2_3_9; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007969; 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; Aldolase class I; 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 NCBIfam; TIGR00419; tim; 1.
DR PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00147};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00147};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00147}.
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
SQ SEQUENCE 248 AA; 27323 MW; 93F7DDFEA277AE2E CRC64;
MRKAIIAGNW KMNKNLEDAL ELVEELKPLV RGAKCDVVLC PPYVCLDAVV KSVGGTNIKV
GAQNMHYEES GAYTGEISPG MLKSLKVDYV IIGHSERRQY FNEKDETINK KIKKAFEHDI
IPIVCCGESL LERENGITEE VLGRQIKLAL KDLRKEQVEK IVIAYEPIWA IGTGKTATDK
QANDTIAHIR GVVSKMYGEN AAEVVRIQYG GSVKPATIKA QMEQPHIDGA LVGGASLKPQ
DFAAIVNY
//
