TPIS_STRP2
ID TPIS_STRP2 Reviewed; 252 AA.
AC Q04JH4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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}; OrderedLocusNames=SPD_1404;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ55094.1; -; Genomic_DNA.
DR RefSeq; WP_000087897.1; NC_008533.2.
DR PDB; 5IBX; X-ray; 1.65 A; A/B/C/D/E/F/G/H=1-252.
DR PDBsum; 5IBX; -.
DR AlphaFoldDB; Q04JH4; -.
DR SMR; Q04JH4; -.
DR STRING; 373153.SPD_1404; -.
DR EnsemblBacteria; ABJ55094; ABJ55094; SPD_1404.
DR GeneID; 60234111; -.
DR GeneID; 66806665; -.
DR KEGG; spd:SPD_1404; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_3_9; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1266295at2; -.
DR BioCyc; SPNE373153:G1G6V-1510-MON; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001452; 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.
FT CHAIN 1..252
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000307572"
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 STRAND 6..10
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5IBX"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 181..199
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5IBX"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:5IBX"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5IBX"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:5IBX"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:5IBX"
SQ SEQUENCE 252 AA; 26550 MW; 8B6493EF645DE62F CRC64;
MSRKPFIAGN WKMNKNPEEA KAFVEAVASK LPSSDLVEAG IAAPALDLTT VLAVAKGSNL
KVAAQNCYFE NAGAFTGETS PQVLKEIGTD YVVIGHSERR DYFHETDEDI NKKAKAIFAN
GMLPIICCGE SLETYEAGKA AEFVGAQVSA ALAGLTAEQV AASVIAYEPI WAIGTGKSAS
QDDAQKMCKV VRDVVAADFG QEVADKVRVQ YGGSVKPENV ASYMACPDVD GALVGGASLE
AESFLALLDF VK
