TPIS_STRCO
ID TPIS_STRCO Reviewed; 258 AA.
AC Q9Z520;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:26206330};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:26206330};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:26206330};
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=SCO1945; ORFNames=SCC54.05c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=13 / Type A;
RX PubMed=26206330; DOI=10.1039/c5cp01599e;
RA Romero-Romero S., Costas M., Rodriguez-Romero A.,
RA Alejandro Fernandez-Velasco D.;
RT "Reversibility and two state behaviour in the thermal unfolding of
RT oligomeric TIM barrel proteins.";
RL Phys. Chem. Chem. Phys. 17:20699-20714(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:26206330}.
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:26206330};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for G3P {ECO:0000269|PubMed:26206330};
CC Note=kcat is 5668 sec(-1) for isomerase activity.
CC {ECO:0000269|PubMed:26206330};
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:26206330}.
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; AL939110; CAB38135.1; -; Genomic_DNA.
DR PIR; T36018; T36018.
DR RefSeq; NP_626209.1; NC_003888.3.
DR RefSeq; WP_003976873.1; NZ_VNID01000001.1.
DR PDB; 4Y9A; X-ray; 2.29 A; A/B/C/D=1-258.
DR PDBsum; 4Y9A; -.
DR AlphaFoldDB; Q9Z520; -.
DR SMR; Q9Z520; -.
DR STRING; 100226.SCO1945; -.
DR PRIDE; Q9Z520; -.
DR GeneID; 1097379; -.
DR KEGG; sco:SCO1945; -.
DR PATRIC; fig|100226.15.peg.1972; -.
DR eggNOG; COG0149; Bacteria.
DR HOGENOM; CLU_024251_2_3_11; -.
DR InParanoid; Q9Z520; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; Q9Z520; -.
DR SABIO-RK; Q9Z520; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001973; 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..258
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090295"
FT ACT_SITE 101
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 240..241
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:4Y9A"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4Y9A"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:4Y9A"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:4Y9A"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:4Y9A"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:4Y9A"
SQ SEQUENCE 258 AA; 27736 MW; 4454F4DF07D34FFA CRC64;
MTTRTPLMAG NWKMNLNHLE AIAHVQKLAF ALADKDYDAV EVAVLAPFTD LRSVQTLVDG
DKLKIKYGAQ DISAHDGGAY TGEISGPMLA KLKCTYVAVG HSERRQYHAE TDEIVNAKVK
AAYKHGLTPI LCVGEELDVR EAGNHVEHTL AQVEGGLKDL AAEQAESVVI AYEPVWAIGT
GKVCGADDAQ EVCAAIRGKL AELYSQELAD KVRIQYGGSV KSGNVAEIMA KPDIDGALVG
GASLDSDEFV KIVRFRDQ
