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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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
//