TPIS_BARHE
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 03-AUG-2022, entry version 116.
DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147};
DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147};
DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147};
DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147};
GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=BH05680;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX 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 / DSM 28221 / 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 derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), AND SUBUNIT.
RA Abendroth J., Edwards T.E., Staker B.;
RT "Crystal structure of triosephosphate isomerase from Bartonella henselae at
RT 1.6A resolution.";
RL Submitted (DEC-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00147}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00147}.
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DR EMBL; AY074775; AAL74288.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF27376.1; -; Genomic_DNA.
DR RefSeq; WP_011180497.1; NZ_LRIJ02000001.1.
DR PDB; 3KXQ; X-ray; 1.60 A; A/B=1-254.
DR PDBsum; 3KXQ; -.
DR AlphaFoldDB; Q8L1Z5; -.
DR SMR; Q8L1Z5; -.
DR STRING; 283166.BH05680; -.
DR PaxDb; Q8L1Z5; -.
DR PRIDE; Q8L1Z5; -.
DR EnsemblBacteria; CAF27376; CAF27376; BH05680.
DR GeneID; 64156847; -.
DR KEGG; bhe:BH05680; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; QEVCGAI; -.
DR BRENDA; 5.3.1.1; 7854.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q8L1Z5; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
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; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..254
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090181"
FT ACT_SITE 99
FT /note="Electrophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00147"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3KXQ"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:3KXQ"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 182..204
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3KXQ"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3KXQ"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:3KXQ"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3KXQ"
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
