TPIS_LACLA
ID TPIS_LACLA Reviewed; 252 AA.
AC P50918; Q9CGG2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
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=LL1134; ORFNames=L0006;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-38.
RC STRAIN=LM0230;
RX PubMed=7534588; DOI=10.1099/00221287-141-1-229;
RA Cancilla M.R., Davidson B.E., Hillier A.J., Nguyen N.Y., Thompson J.;
RT "The Lactococcus lactis triosephosphate isomerase gene, tpi, is
RT monocistronic.";
RL Microbiology 141:229-238(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; U07640; AAC43268.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05232.1; -; Genomic_DNA.
DR PIR; F86766; F86766.
DR RefSeq; NP_267290.1; NC_002662.1.
DR RefSeq; WP_003132078.1; NC_002662.1.
DR AlphaFoldDB; P50918; -.
DR SMR; P50918; -.
DR STRING; 272623.L0006; -.
DR PaxDb; P50918; -.
DR EnsemblBacteria; AAK05232; AAK05232; L0006.
DR KEGG; lla:L0006; -.
DR PATRIC; fig|272623.7.peg.1212; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_3_9; -.
DR OMA; QEVCGAI; -.
DR BioCyc; MetaCyc:MON-13055; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002196; 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 Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7534588"
FT CHAIN 2..252
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090233"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 168
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 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT CONFLICT 89
FT /note="V -> I (in Ref. 1; AAC43268)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> T (in Ref. 1; AAC43268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 26905 MW; D19B58BE0E8892D3 CRC64;
MSRKPIIAGN WKMNKTLSEA QAFVEAVKNN LPSSDNVESV IGAPALFLAP MAYLRQGSEL
KLAAENSYFE NAGAFTGENS PAAIVDLGVE YIIIGHSERR EYFHETDEDI NKKAKAIFAA
GATPILCCGE TLETFEAGKT AEWVSGQIEA GLAGLSAEQV SNLVIAYEPI WAIGTGKTAT
NEIADETCGV VRSTVEKLYG KEVSEAVRIQ YGGSVKPETI EGLMAKENID GALVGGASLE
ADSFLALLEM YK
