TPIS_METJA
ID TPIS_METJA Reviewed; 219 AA.
AC Q58923;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17242514};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17242514};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17242514};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=MJ1528;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-219, FUNCTION AS A
RP TRIOSEPHOSPHATE ISOMERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=17242514; DOI=10.1107/s0907444906046488;
RA Gayathri P., Banerjee M., Vijayalakshmi A., Azeez S., Balaram H.,
RA Balaram P., Murthy M.R.;
RT "Structure of triosephosphate isomerase (TIM) from Methanocaldococcus
RT jannaschii.";
RL Acta Crystallogr. D 63:206-220(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 ECO:0000269|PubMed:17242514}.
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 ECO:0000269|PubMed:17242514};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC The enzyme is active over the temperature range 20-60 degrees
CC Celsius, showing an increase in specific activity with temperature.
CC {ECO:0000269|PubMed:17242514};
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: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00147, ECO:0000269|PubMed:17242514}.
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; L77117; AAB99546.1; -; Genomic_DNA.
DR PIR; G64490; G64490.
DR RefSeq; WP_010871052.1; NC_000909.1.
DR PDB; 2H6R; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-219.
DR PDBsum; 2H6R; -.
DR AlphaFoldDB; Q58923; -.
DR SMR; Q58923; -.
DR STRING; 243232.MJ_1528; -.
DR EnsemblBacteria; AAB99546; AAB99546; MJ_1528.
DR GeneID; 1452436; -.
DR KEGG; mja:MJ_1528; -.
DR eggNOG; arCOG01087; Archaea.
DR HOGENOM; CLU_104921_0_0_2; -.
DR InParanoid; Q58923; -.
DR OMA; IPVYAQH; -.
DR OrthoDB; 60670at2157; -.
DR PhylomeDB; Q58923; -.
DR BioCyc; MetaCyc:MON-14589; -.
DR BRENDA; 5.3.1.1; 3260.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q58923; -.
DR Proteomes; UP000000805; 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_A; TIM_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR022891; Triosephosphate_isomerase_arc.
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..219
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090335"
FT ACT_SITE 90
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 6..8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 143
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 199..200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2H6R"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2H6R"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2H6R"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2H6R"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2H6R"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:2H6R"
SQ SEQUENCE 219 AA; 23319 MW; C6BC49A2DEE8A026 CRC64;
MLIVINYKTY NESIGNRGLE IAKIAEKVSE ESGITIGVAP QFVDLRMIVE NVNIPVYAQH
IDNINPGSHT GHILAEAIKD CGCKGTLINH SEKRMLLADI EAVINKCKNL GLETIVCTNN
INTSKAVAAL SPDYIAVEPP ELIGTGIPVS KANPEVVEGT VRAVKEINKD VKVLCGAGIS
KGEDVKAALD LGAEGVLLAS GVVKAKNVEE AIRELIKFI
