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Database: UniProt/SWISS-PROT
Entry: TPIS_ROSCS
LinkDB: TPIS_ROSCS
Original site: TPIS_ROSCS 
ID   TPIS_ROSCS              Reviewed;         254 AA.
AC   A7NI03;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   28-MAR-2018, entry version 70.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
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};
GN   OrderedLocusNames=Rcas_0991;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Hanada S.,
RA   Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00147}.
DR   EMBL; CP000804; ABU57100.1; -; Genomic_DNA.
DR   RefSeq; WP_012119530.1; NC_009767.1.
DR   ProteinModelPortal; A7NI03; -.
DR   SMR; A7NI03; -.
DR   STRING; 383372.Rcas_0991; -.
DR   EnsemblBacteria; ABU57100; ABU57100; Rcas_0991.
DR   KEGG; rca:Rcas_0991; -.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   OrthoDB; POG091H02GL; -.
DR   BioCyc; RCAS383372:G1G9S-1042-MONOMER; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000263; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    254       Triosephosphate isomerase.
FT                                /FTId=PRO_1000076657.
FT   REGION        9     11       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      234    235       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE     95     95       Electrophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    167    167       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   BINDING     173    173       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00147}.
FT   BINDING     213    213       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
SQ   SEQUENCE   254 AA;  26913 MW;  5F0CFB51E151B9DA CRC64;
     MRTPLLAGNW KMYKTTGEAR ELVEGLLHGL GDVGDRKVLV CPPFTALQTV HDLVQGTPIA
     LGAQDVYIEP QGAFTGAISP VMLRDLGCAY VIVGHSERRA IFGEGDELIG KKVRAALAHD
     LTPILCVGET KPQRDAGHAE TVVVAQVRAA LTGMTPEQIG RIVIAYEPVW AIGTGDTATP
     ADAQAMHETI RRILGDMAGS DTAATINILY GGSVKPDNID DLMAQPDIDG ALVGGASLKA
     DSFLRIVHFL SPQE
//
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