TPIS_DEIRA
ID TPIS_DEIRA Reviewed; 244 AA.
AC Q9RUP5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
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}; OrderedLocusNames=DR_1339;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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=0.69 mM for G3P {ECO:0000269|PubMed:26206330};
CC Note=kcat is 5678 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; AE000513; AAF10911.1; -; Genomic_DNA.
DR PIR; A75408; A75408.
DR RefSeq; NP_295062.1; NC_001263.1.
DR PDB; 4Y90; X-ray; 2.10 A; A/B/C/D=1-244.
DR PDBsum; 4Y90; -.
DR SMR; Q9RUP5; -.
DR STRING; 243230.DR_1339; -.
DR EnsemblBacteria; AAF10911; AAF10911; DR_1339.
DR KEGG; dra:DR_1339; -.
DR PATRIC; fig|243230.17.peg.1536; -.
DR eggNOG; COG0149; Bacteria.
DR InParanoid; Q9RUP5; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1266295at2; -.
DR SABIO-RK; Q9RUP5; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002524; Chromosome I.
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..244
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090216"
FT ACT_SITE 93
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 227..228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:4Y90"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:4Y90"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4Y90"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:4Y90"
SQ SEQUENCE 244 AA; 25322 MW; 42FADCB2114788FB CRC64;
MQTLLALNWK MNKTPTEARS WAEELTTKYA PAEGVDLAVL APALDLSALA ANLPAGIAFG
GQDVSAHESG AYTGEISAAM LKDAGASCVV VGHSERREYH DESDAXVAAK ARQAQANGLL
PIVCVGENLD VRERGEHVPQ TLAQLRGSLE GVGADVVVAY EPVWAIGTGK TATADDAEEL
AAAIRGALRE QYGARAEGIR VLYGGSVKPE NIAEICGKPN VNGALVGGAS LKVPDVLGML
DALR
