TPIS_SCYPA
ID TPIS_SCYPA Reviewed; 248 AA.
AC A0A1L5YRA2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013, ECO:0000303|PubMed:31668066};
DE Short=TIM {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000303|PubMed:30187588, ECO:0000303|PubMed:31668066};
DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013};
DE AltName: Full=Allergen Scy p 8 {ECO:0000303|PubMed:31668066};
DE AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939};
DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|PROSITE-ProRule:PRU10127};
DE AltName: Allergen=Scy p 8.0101 {ECO:0000305};
OS Scylla paramamosain (Mud crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Scylla.
OX NCBI_TaxID=85552 {ECO:0000312|EMBL:APP94292.1};
RN [1] {ECO:0000312|EMBL:APP94292.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang Y.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=30187588; DOI=10.1111/cea.13266;
RA Yang Y., Hu M.J., Jin T.C., Zhang Y.X., Liu G.Y., Li Y.B., Zhang M.L.,
RA Cao M.J., Su W.J., Liu G.M.;
RT "A comprehensive analysis of the allergenicity and IgE epitopes of
RT myosinogen allergens in Scylla paramamosain.";
RL Clin. Exp. Allergy 49:108-119(2019).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, ALLERGEN, MUTAGENESIS OF
RP TRP-168; THR-172; GLN-180 AND LYS-237, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=31668066; DOI=10.1021/acs.jafc.9b05279;
RA Xia F., Li M.S., Liu Q.M., Liu M., Yang Y., Cao M.J., Chen G.X., Jin T.,
RA Liu G.M.;
RT "Crystal Structure Analysis and Conformational Epitope Mutation of
RT Triosephosphate Isomerase, a Mud Crab Allergen.";
RL J. Agric. Food Chem. 67:12918-12926(2019).
CC -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic
CC enzyme that catalyzes the interconversion between dihydroxyacetone
CC phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis
CC and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.
CC -!- FUNCTION: It is also responsible for the non-negligible production of
CC methylglyoxal a reactive cytotoxic side-product that modifies and can
CC alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.
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|PROSITE-ProRule:PRU10127,
CC ECO:0000255|RuleBase:RU363013};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642; EC=4.2.3.3;
CC Evidence={ECO:0000250|UniProtKB:P00939};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127,
CC ECO:0000269|PubMed:31668066}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:30187588}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to crabs (PubMed:30187588, PubMed:31668066). Binds to
CC IgE in 23% of the 30 patients tested (PubMed:30187588). Binds to IgE in
CC all 12 patients tested. Induces activation of human basophils
CC (PubMed:31668066). {ECO:0000269|PubMed:30187588,
CC ECO:0000269|PubMed:31668066}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.
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DR EMBL; KX083344; APP94292.1; -; mRNA.
DR PDB; 6JOX; X-ray; 1.80 A; A/B=1-248.
DR PDBsum; 6JOX; -.
DR AlphaFoldDB; A0A1L5YRA2; -.
DR SMR; A0A1L5YRA2; -.
DR Allergome; 12151; Scy p 8.
DR Allergome; 12152; Scy p 8.0101.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0008929; F:methylglyoxal synthase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; ISS:UniProtKB.
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; Allergen; Cytoplasm; Gluconeogenesis; Glycolysis;
KW IgE-binding protein; Isomerase; Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00940"
FT CHAIN 2..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000449136"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT MUTAGEN 168
FT /note="W->A: Reduced IgE-binding activity by approximately
FT 30% compared to wild-type, but still induces human basophil
FT activation."
FT /evidence="ECO:0000269|PubMed:31668066"
FT MUTAGEN 172
FT /note="T->A: Subtle increased IgE-binding activity compared
FT to wild-type."
FT /evidence="ECO:0000269|PubMed:31668066"
FT MUTAGEN 180
FT /note="Q->A: Subtle increased IgE-binding activity compared
FT to wild-type."
FT /evidence="ECO:0000269|PubMed:31668066"
FT MUTAGEN 237
FT /note="K->A: Reduced IgE-binding activity by approximately
FT 30% compared to wild-type, but still induces human basophil
FT activation."
FT /evidence="ECO:0000269|PubMed:31668066"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6JOX"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6JOX"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6JOX"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:6JOX"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:6JOX"
SQ SEQUENCE 248 AA; 26974 MW; C7C9558E2085F7C3 CRC64;
MANQRKFFVG GNWKMNGDKA AIDGIISFMK GPLNADTEVV VGCPQCYLMY TREHMPANIG
VAAQNCYKTA KGAFTGEISP AMIKDCGCEW VILGHSERRN VFGEPDQLIS EKVGHALEAG
LKVIPCIGEK LEERESNRTE EVVFAQMKAL VPNISDWSRV VIAYEPVWAI GTGKTATPEQ
AQDVHAKLRQ WLRDNVSPQV AESTRIIYGG SVSAGNCKEL AKTGDIDGFL VGGASLKPDF
VTIINARA
