TPIS_STAAR
ID TPIS_STAAR Reviewed; 253 AA.
AC Q6GIL6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:22813930};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:22813930};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:22813930};
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=SAR0830;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP FUNCTION.
RX PubMed=11425708; DOI=10.1128/aem.67.7.2958-2965.2001;
RA Becker P., Hufnagle W., Peters G., Herrmann M.;
RT "Detection of differential gene expression in biofilm-forming versus
RT planktonic populations of Staphylococcus aureus using micro-
RT representational-difference analysis.";
RL Appl. Environ. Microbiol. 67:2958-2965(2001).
RN [3]
RP FUNCTION.
RX PubMed=22003920; DOI=10.1111/j.1348-0421.2011.00392.x;
RA Furuya H., Ikeda R.;
RT "Interaction of triosephosphate isomerase from Staphylococcus aureus with
RT plasminogen.";
RL Microbiol. Immunol. 55:855-862(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP SUBSTRATE ANALOGS, AND SUBUNIT.
RX PubMed=22813930; DOI=10.1016/j.biochi.2012.07.001;
RA Mukherjee S., Roychowdhury A., Dutta D., Das A.K.;
RT "Crystal structures of triosephosphate isomerase from methicillin resistant
RT Staphylococcus aureus MRSA252 provide structural insights into novel modes
RT of ligand binding and unique conformations of catalytic loop.";
RL Biochimie 94:2532-2544(2012).
CC -!- FUNCTION: Involved in biofilm formation (PubMed:11425708). It also
CC plays an instrumental role in adherence and invasion of the bacteria
CC into the host cell (PubMed:22003920). Catalyzes stereospecifically the
CC conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-
CC phosphate (G3P). It binds plasminogen. {ECO:0000269|PubMed:11425708,
CC ECO:0000269|PubMed:22003920}.
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 ECO:0000269|PubMed:22813930}.
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; BX571856; CAG39839.1; -; Genomic_DNA.
DR RefSeq; WP_001260089.1; NC_002952.2.
DR PDB; 3M9Y; X-ray; 1.90 A; A/B=1-253.
DR PDB; 3UWU; X-ray; 2.15 A; A/B=1-253.
DR PDB; 3UWV; X-ray; 2.07 A; A/B=1-253.
DR PDB; 3UWW; X-ray; 2.25 A; A/B=1-253.
DR PDB; 3UWY; X-ray; 2.40 A; A/B=1-253.
DR PDB; 3UWZ; X-ray; 2.50 A; A/B=1-253.
DR PDBsum; 3M9Y; -.
DR PDBsum; 3UWU; -.
DR PDBsum; 3UWV; -.
DR PDBsum; 3UWW; -.
DR PDBsum; 3UWY; -.
DR PDBsum; 3UWZ; -.
DR AlphaFoldDB; Q6GIL6; -.
DR SMR; Q6GIL6; -.
DR MoonProt; Q6GIL6; -.
DR KEGG; sar:SAR0830; -.
DR HOGENOM; CLU_024251_2_3_9; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1266295at2; -.
DR BRENDA; 5.3.1.1; 3352.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000596; 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; Virulence.
FT CHAIN 1..253
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090286"
FT ACT_SITE 97
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000305|PubMed:22813930"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000305|PubMed:22813930"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22813930"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22813930"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22813930"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22813930"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3M9Y"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:3M9Y"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:3UWV"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3UWV"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3M9Y"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3M9Y"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3M9Y"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:3M9Y"
SQ SEQUENCE 253 AA; 27262 MW; 7B35B772F736DEAD CRC64;
MRTPIIAGNW KMNKTVQEAK DFVNALPTLP DSKEVESVIC APAIQLDALT TAVKEGKAQG
LEIGAQNTYF EDNGAFTGET SPVALADLGV KYVVIGHSER RELFHETDEE INKKAHAIFK
HGMTPIICVG ETDEERESGK ANDVVGEQVK KAVAGLSEDQ LKSVVIAYEP IWAIGTGKSS
TSEDANEMCA FVRQTIADLS SKEVSEATRI QYGGSVKPNN IKEYMAQTDI DGALVGGASL
KVEDFVQLLE GAK
