GenomeNet

Database: UniProt
Entry: Q8YCV3
LinkDB: Q8YCV3
Original site: Q8YCV3 
ID   TPIS2_BRUME             Reviewed;         256 AA.
AC   Q8YCV3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-MAR-2016, entry version 90.
DE   RecName: Full=Triosephosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TIM 2 {ECO:0000255|HAMAP-Rule:MF_00147};
DE            Short=TPI 2 {ECO:0000255|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE   AltName: Full=Triose-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00147};
GN   Name=tpiA2 {ECO:0000255|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=BMEII0425;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53667.1; -; Genomic_DNA.
DR   PIR; AH3562; AH3562.
DR   RefSeq; WP_004682245.1; NZ_GG703779.1.
DR   ProteinModelPortal; Q8YCV3; -.
DR   STRING; 224914.BAWG_2141; -.
DR   EnsemblBacteria; AAL53667; AAL53667; BMEII0425.
DR   KEGG; bme:BMEII0425; -.
DR   PATRIC; 17800280; VBIBruMel146950_2473.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; FAHEIDG; -.
DR   OrthoDB; EOG66QM23; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Pentose shunt.
FT   CHAIN         1    256       Triosephosphate isomerase 2.
FT                                /FTId=PRO_0000090192.
FT   ACT_SITE     96     96       Electrophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE    169    169       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
FT   BINDING     175    175       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00147}.
FT   BINDING     212    212       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00147}.
SQ   SEQUENCE   256 AA;  27848 MW;  89F049D4B1306707 CRC64;
     MTKFWIGTSW KMNKTLAEAR LFAEALKAAD AGRSPDIQRF VIPPFTAVRE VKEILSGTSV
     KVGAQNMHWA DQGTWTGEIS PLMLKDCNLD IVELGHSERR EHFGETNETV GLKVEAAVRH
     GLIPLICIGE TLEDCESGRA AAVLEEEVRG ALSKLSEAQK QAEILFAYEP VWAIGENGIP
     ASADYADARQ AEIIAVAQSV LARRVPCLYG GSVNPGNCEE LIACPHIDGL FIGRSAWNVE
     GYLDILARCA TKVQAN
//
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