ID   TPIS_BARHE              Reviewed;         254 AA.
AC   Q8L1Z5;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA; OrderedLocusNames=BH05680;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   MEDLINE=21980668; PubMed=11983902; DOI=10.1073/pnas.082112499;
RA   Canback B., Andersson S.G.E., Kurland C.G.;
RT   "The global phylogeny of glycolytic enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6097-6102(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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.
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DR   EMBL; AY074775; AAL74288.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27376.1; -; Genomic_DNA.
DR   RefSeq; YP_033402.1; -.
DR   HSSP; P36204; 1B9B.
DR   GeneID; 2865236; -.
DR   GenomeReviews; BX897699_GR; BH05680.
DR   KEGG; bhe:BH05680; -.
DR   NMPDR; fig|283166.1.peg.530; -.
DR   HOGENOM; Q8L1Z5; -.
DR   OMA; Q8L1Z5; NFKMNGT.
DR   BioCyc; BHEN283166:BH05680-MON; -.
DR   BRENDA; 5.3.1.1; 277357.
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; 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    254       Triosephosphate isomerase.
FT                                /FTId=PRO_0000090181.
FT   ACT_SITE     99     99       Electrophile (By similarity).
FT   ACT_SITE    169    169       Proton acceptor (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
FT   BINDING      14     14       Substrate (By similarity).
SQ   SEQUENCE   254 AA;  27165 MW;  50BB63614C90769F CRC64;
     MSPNIRPFIA GNWKMNGTGE SLGELRAIAA GISSDLGRLF EALICVPATL LSRAFDILGG
     ENILLGGQNC HFDDYGPYTG DISAFMLKEA GASHVIIGHS ERRTVYQESD AIVRAKVQAA
     WRAGLVALIC VGETLEERKS NKVLDVLTRQ LEGSLPDGAT AENIIIAYEP VWAVGTGNTA
     TSADVAEVHA FIHHKMHSRF GDEGAKIRLL YGGSVKPSNA FELLSTAHVN GALIGGASLK
     AIDFLTICDV YRKL
//