ID   TPIS_BAUCH              Reviewed;         256 AA.
AC   Q1LTT4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, 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=BCI_0169;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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 (Probable).
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; CP000238; ABF13817.1; -; Genomic_DNA.
DR   RefSeq; YP_588630.1; -.
DR   GeneID; 4056146; -.
DR   GenomeReviews; CP000238_GR; BCI_0169.
DR   KEGG; bci:BCI_0169; -.
DR   HOGENOM; Q1LTT4; -.
DR   OMA; Q1LTT4; NFKMNGT.
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   HAMAP; MF_00147; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR21139; Triophos_ismrse; 1.
DR   Pfam; PF00121; TIM; 1.
DR   ProDom; PD001005; Triophos_ismrse; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; FALSE_NEG.
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.
FT                                /FTId=PRO_0000307435.
FT   ACT_SITE     96     96       Electrophile (By similarity).
FT   ACT_SITE    168    168       Proton acceptor (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
SQ   SEQUENCE   256 AA;  28116 MW;  87C95FCA02A9DF38 CRC64;
     MRHPLVIGNW KLNGSKHMVS NFIISLRNQL SNMINCCNVA IAPPMIYLDR AKSYLTGSHI
     ALGAQNVDLH VSGAFTGEIS AKMLKDIGAK YIIIGHIERR LYHKESNEDI ANKFACLKNE
     GLIPVLCIGE TKEENEKDQT KAICVRQLDY ILNIVGTQAF KNAVIAYEPI WAIATGKSAN
     PLQIQKIHKF IRSYLFNHDQ AIAEQVIIQY GGSVNASNAA ELFNQPDVDG ALVGGASLKA
     DIFATIIKAA ARAKKN
//