ID   TPIS_ALCBS              Reviewed;         247 AA.
AC   Q0VSS5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=tpiA; OrderedLocusNames=ABO_0325;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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.
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DR   EMBL; AM286690; CAL15773.1; -; Genomic_DNA.
DR   RefSeq; YP_692045.1; -.
DR   GeneID; 4211921; -.
DR   GenomeReviews; AM286690_GR; ABO_0325.
DR   KEGG; abo:ABO_0325; -.
DR   NMPDR; fig|393595.12.peg.324; -.
DR   HOGENOM; Q0VSS5; -.
DR   OMA; Q0VSS5; IGAQDCH.
DR   BioCyc; ABOR393595:ABO_0325-MON; -.
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    247       Triosephosphate isomerase.
FT                                /FTId=PRO_0000307421.
FT   ACT_SITE     92     92       Electrophile (By similarity).
FT   ACT_SITE    164    164       Proton acceptor (By similarity).
FT   BINDING      10     10       Substrate (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
SQ   SEQUENCE   247 AA;  25415 MW;  951CC6FA7F9A4DCD CRC64;
     MNRTPLVAGN WKMNGRKDLL TEMADALAGY AGAAEVVICP PFPYLAAARS AMPGAVGIGS
     QNVSEQEDGA FTGEVSAPML AEVGCGYVII GHSERRALYG ETDAQIASKF AHAQAAGLVP
     ILCVGETLEE RDSGNTDTIV CGQLRAVVDA VGVAAFANAI VAYEPVWAIG TGKTASPEQA
     QAVHACLRQF LAKDDPDIAQ SLRLLYGGSV KADNAALLFA QSDIDGGLIG GASLTADSFI
     AICQAAE
//