TPIS_SYNY3
ID TPIS_SYNY3 Reviewed; 242 AA.
AC Q59994;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=slr0783;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10145.1; -; Genomic_DNA.
DR PIR; S76293; S76293.
DR PDB; 6BVE; X-ray; 1.78 A; A/B=1-242.
DR PDBsum; 6BVE; -.
DR AlphaFoldDB; Q59994; -.
DR SMR; Q59994; -.
DR STRING; 1148.1001518; -.
DR PaxDb; Q59994; -.
DR PRIDE; Q59994; -.
DR EnsemblBacteria; BAA10145; BAA10145; BAA10145.
DR KEGG; syn:slr0783; -.
DR eggNOG; COG0149; Bacteria.
DR InParanoid; Q59994; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; Q59994; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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..242
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090306"
FT ACT_SITE 96
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 165
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 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:6BVE"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6BVE"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6BVE"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6BVE"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6BVE"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:6BVE"
SQ SEQUENCE 242 AA; 26159 MW; C418BB2048113AF7 CRC64;
MRKIIIAGNW KMHKTQAEAQ AFLQGFKPLI EDAAESREVV LCVPFTDLSG MSQQLHGGRV
RLGAQNVHWE ASGAYTGEIS AAMLTEIGIH YVVIGHSERR QYFGETDETA NLRVLAAQKA
GLIPILCVGE SKAQRDAGET EQVIVDQVKK GLVNVDQSNL VIAYEPIWAI GTGDTCAATE
ANRVIGLIRE QLTNSQVTIQ YGGSVNANNV DEIMAQPEID GALVGGASLE PQSFARIVNF
QP
