TPIS_MYCTU
ID TPIS_MYCTU Reviewed; 261 AA.
AC P9WG43; L0T6V2; O08408; P66940;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:16978361};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:16978361};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:22120738};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:16978361, ECO:0000269|PubMed:22120738};
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=Rv1438; ORFNames=MTCY493.16c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, AND SUBUNIT.
RX PubMed=16978361; DOI=10.1111/j.1574-6968.2006.00420.x;
RA Mathur D., Malik G., Garg L.C.;
RT "Biochemical and functional characterization of triosephosphate isomerase
RT from Mycobacterium tuberculosis H37Rv.";
RL FEMS Microbiol. Lett. 263:229-235(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=22120738; DOI=10.1107/s0907444911042971;
RA Connor S.E., Capodagli G.C., Deaton M.K., Pegan S.D.;
RT "Structural and functional characterization of Mycobacterium tuberculosis
RT triosephosphate isomerase.";
RL Acta Crystallogr. D 67:1017-1022(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-261 IN COMPLEX WITH SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=25613812; DOI=10.1016/j.tube.2014.12.003;
RA Baugh L., Phan I., Begley D.W., Clifton M.C., Armour B., Dranow D.M.,
RA Taylor B.M., Muruthi M.M., Abendroth J., Fairman J.W., Fox D. III,
RA Dieterich S.H., Staker B.L., Gardberg A.S., Choi R., Hewitt S.N.,
RA Napuli A.J., Myers J., Barrett L.K., Zhang Y., Ferrell M., Mundt E.,
RA Thompkins K., Tran N., Lyons-Abbott S., Abramov A., Sekar A.,
RA Serbzhinskiy D., Lorimer D., Buchko G.W., Stacy R., Stewart L.J.,
RA Edwards T.E., Van Voorhis W.C., Myler P.J.;
RT "Increasing the structural coverage of tuberculosis drug targets.";
RL Tuberculosis 95:142-148(2015).
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:16978361, ECO:0000269|PubMed:22120738}.
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:16978361, ECO:0000269|PubMed:22120738};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for DHAP {ECO:0000269|PubMed:22120738};
CC KM=84 uM for G3P {ECO:0000269|PubMed:16978361};
CC Vmax=39 umol/min/mg enzyme {ECO:0000269|PubMed:16978361};
CC Note=kcat is 4.3 min(-1) for isomerase activity.
CC {ECO:0000269|PubMed:22120738};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:16978361};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. The enzyme is stable up to
CC 50 degrees Celsius. At 55 degrees Celsius, the enzyme retains
CC approximately half of its activity but it is completely inactivated
CC at 60 degrees Celsius. {ECO:0000269|PubMed:16978361};
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:16978361, ECO:0000269|PubMed:22120738,
CC ECO:0000269|PubMed:25613812}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- MASS SPECTROMETRY: Mass=28213; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16978361};
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR EMBL; AL123456; CCP44197.1; -; Genomic_DNA.
DR PIR; A70916; A70916.
DR RefSeq; NP_215954.1; NC_000962.3.
DR RefSeq; WP_003407398.1; NZ_NVQJ01000038.1.
DR PDB; 3GVG; X-ray; 1.55 A; A/B=2-261.
DR PDB; 3TA6; X-ray; 1.41 A; A/B=1-261.
DR PDB; 3TAO; X-ray; 1.45 A; A/B=1-261.
DR PDBsum; 3GVG; -.
DR PDBsum; 3TA6; -.
DR PDBsum; 3TAO; -.
DR AlphaFoldDB; P9WG43; -.
DR SMR; P9WG43; -.
DR STRING; 83332.Rv1438; -.
DR PaxDb; P9WG43; -.
DR DNASU; 886628; -.
DR GeneID; 886628; -.
DR KEGG; mtu:Rv1438; -.
DR TubercuList; Rv1438; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; QEVCGAI; -.
DR PhylomeDB; P9WG43; -.
DR BRENDA; 5.3.1.1; 3445.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:MTBBASE.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MTBBASE.
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; IDA:MTBBASE.
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..261
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090256"
FT ACT_SITE 100
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000305|PubMed:22120738, ECO:0000305|PubMed:25613812"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000305|PubMed:25613812"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22120738, ECO:0000269|PubMed:25613812"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22120738"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22120738"
FT BINDING 239..240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147,
FT ECO:0000269|PubMed:22120738"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3TA6"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3TA6"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:3TA6"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:3TA6"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:3TA6"
SQ SEQUENCE 261 AA; 27403 MW; 3559BAA35031E471 CRC64;
MSRKPLIAGN WKMNLNHYEA IALVQKIAFS LPDKYYDRVD VAVIPPFTDL RSVQTLVDGD
KLRLTYGAQD LSPHDSGAYT GDVSGAFLAK LGCSYVVVGH SERRTYHNED DALVAAKAAT
ALKHGLTPIV CIGEHLDVRE AGNHVAHNIE QLRGSLAGLL AEQIGSVVIA YEPVWAIGTG
RVASAADAQE VCAAIRKELA SLASPRIADT VRVLYGGSVN AKNVGDIVAQ DDVDGGLVGG
ASLDGEHFAT LAAIAAGGPL P
