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Database: UniProt/TrEMBL
Entry: E0U2U8_BACPZ
LinkDB: E0U2U8_BACPZ
Original site: E0U2U8_BACPZ 
ID   E0U2U8_BACPZ            Unreviewed;       253 AA.
AC   E0U2U8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   01-MAY-2013, entry version 21.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA; OrderedLocusNames=BSUW23_16660;
OS   Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472
OS   / W23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA   Zeigler D.R.;
RT   "Complete genome sequence of Bacillus subtilis subsp. spizizenii str.
RT   W23.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W23;
RA   Zeigler D.R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002183; ADM39367.1; -; Genomic_DNA.
DR   RefSeq; YP_003867676.1; NC_014479.1.
DR   EnsemblBacteria; ADM39367; ADM39367; BSUW23_16660.
DR   GeneID; 9724339; -.
DR   KEGG; bss:BSUW23_16660; -.
DR   PATRIC; 42192898; VBIBacSub57968_3397.
DR   HOGENOM; HOG000226412; -.
DR   KO; K01803; -.
DR   OMA; QEVCGAI; -.
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; Phosphoprotein.
FT   ACT_SITE     95     95       Electrophile (By similarity).
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
SQ   SEQUENCE   253 AA;  27088 MW;  CD1CD9563A0A3595 CRC64;
     MRKPIIAGNW KMNKTLGEAV SFVEEVKSSI PAADKAEAVV CAPALFLEKL TSAVKGTDLK
     VGAQNMHFEE SGAFTGEISP VALKDLGVDY CVIGHSERRE MFAETDETVN KKAHAAFKHG
     IVPIICVGET LEEREAGKTN DLVADQVKKG LAGLSEEQVA ASVIAYEPIW AIGTGKSSTA
     KDANDVCAHI RKTVAESFSQ EVADKLRIQY GGSVKPANIK EYMAESDIDG ALVGGASLEP
     QSFVQLLEEG QYE
//
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