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Database: UniProt/TrEMBL
Entry: B8ZLT6_STRPJ
LinkDB: B8ZLT6_STRPJ
Original site: B8ZLT6_STRPJ 
ID   B8ZLT6_STRPJ            Unreviewed;       252 AA.
AC   B8ZLT6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   01-MAY-2013, entry version 30.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpi; Synonyms=tpiA; OrderedLocusNames=SPN23F15910;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/JB.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K.,
RA   Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J.,
RA   Bentley S.D., Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-
RT   resistant pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR69369.1; -; Genomic_DNA.
DR   RefSeq; YP_002511488.1; NC_011900.1.
DR   ProteinModelPortal; B8ZLT6; -.
DR   SMR; B8ZLT6; 3-251.
DR   STRING; 561276.SPN23F_15910; -.
DR   GeneID; 7328798; -.
DR   KEGG; sne:SPN23F_15910; -.
DR   PATRIC; 19674540; VBIStrPne132160_1672.
DR   eggNOG; COG0149; -.
DR   KO; K01803; -.
DR   OMA; ANTVIAY; -.
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:HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA: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; Triophos_ismrse; 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;
KW   Pentose shunt.
FT   ACT_SITE     96     96       Electrophile (By similarity).
FT   ACT_SITE    168    168       Proton acceptor (By similarity).
FT   BINDING      10     10       Substrate (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
SQ   SEQUENCE   252 AA;  26550 MW;  8B6493EF645DE62F CRC64;
     MSRKPFIAGN WKMNKNPEEA KAFVEAVASK LPSSDLVEAG IAAPALDLTT VLAVAKGSNL
     KVAAQNCYFE NAGAFTGETS PQVLKEIGTD YVVIGHSERR DYFHETDEDI NKKAKAIFAN
     GMLPIICCGE SLETYEAGKA AEFVGAQVSA ALAGLTAEQV AASVIAYEPI WAIGTGKSAS
     QDDAQKMCKV VRDVVAADFG QEVADKVRVQ YGGSVKPENV ASYMACPDVD GALVGGASLE
     AESFLALLDF VK
//
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