TPIS_CORGL
ID TPIS_CORGL Reviewed; 259 AA.
AC P19583; Q59287;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
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}; Synonyms=tpi;
GN OrderedLocusNames=Cgl1586, cg1789;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=1400158; DOI=10.1128/jb.174.19.6076-6086.1992;
RA Eikmanns B.J.;
RT "Identification, sequence analysis, and expression of a Corynebacterium
RT glutamicum gene cluster encoding the three glycolytic enzymes
RT glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and
RT triosephosphate isomerase.";
RL J. Bacteriol. 174:6076-6086(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-259.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=2666264; DOI=10.1016/0378-1119(89)90072-3;
RA O'Regan M., Thierbach G., Bachmann B., Villeval D., Lepage P., Viret J.F.,
RA Lemoine Y.;
RT "Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-
RT coding gene of Corynebacterium glutamicum ATCC13032.";
RL Gene 77:237-251(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-259.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2779518; DOI=10.1007/bf00331286;
RA Eikmanns B.J., Follettie M.T., Griot M.U., Sinskey A.J.;
RT "The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum:
RT molecular cloning, nucleotide sequence, and expression.";
RL Mol. Gen. Genet. 218:330-339(1989).
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 -!- 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; X59403; CAA42047.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98979.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21594.1; -; Genomic_DNA.
DR EMBL; M25819; AAA83536.1; -; Genomic_DNA.
DR EMBL; X14234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C43260; C43260.
DR RefSeq; NP_600800.1; NC_003450.3.
DR RefSeq; WP_011014466.1; NC_006958.1.
DR AlphaFoldDB; P19583; -.
DR SMR; P19583; -.
DR STRING; 196627.cg1789; -.
DR World-2DPAGE; 0001:P19583; -.
DR KEGG; cgb:cg1789; -.
DR KEGG; cgl:Cgl1586; -.
DR PATRIC; fig|196627.13.peg.1548; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_3_11; -.
DR OMA; QEVCGAI; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000582; 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 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..259
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090214"
FT ACT_SITE 100
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 239..240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT CONFLICT 248..249
FT /note="FA -> LP (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 27203 MW; 3BC85A368505E57E CRC64;
MARKPLIAGN WKMNLDHQQA IGTVQKLAFA LPKEYFEKVD VAVTVPFTDI RSVQTLVEGD
KLEVTFGAQD VSQHESGAYT GEVSASMLAK LNCSWVVVGH SERREYHNES DELVAAKAKA
ALSNGISPIV CVGEPLEIRE AGTHVEYVVE QTRKSLAGLD AAELANTVIA YEPVWAIGTG
KVASAADAQE VCKAIRGLIV ELAGDEVAEG LRILYGGSVK AETVAEIVGQ PDVDGGLVGG
ASLDGEAFAK LAANAASVA
