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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   19-FEB-2014, entry version 78.
DE   RecName: Full=Triosephosphate isomerase 2;
DE            Short=TIM 2;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase 2;
GN   Name=tpiA2; 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   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
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DR   EMBL; AE008918; AAL53667.1; -; Genomic_DNA.
DR   PIR; AH3562; AH3562.
DR   RefSeq; NP_541403.1; NC_003318.1.
DR   ProteinModelPortal; Q8YCV3; -.
DR   STRING; 224914.BMEII0425; -.
DR   EnsemblBacteria; AAL53667; AAL53667; BMEII0425.
DR   GeneID; 1198197; -.
DR   KEGG; bme:BMEII0425; -.
DR   PATRIC; 17800280; VBIBruMel146950_2473.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; FAHEIDG; -.
DR   OrthoDB; EOG66QM23; -.
DR   ProtClustDB; PRK00042; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
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:glycolysis; 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 (By similarity).
FT   ACT_SITE    169    169       Proton acceptor (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
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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