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Database: UniProt/TrEMBL
Entry: H2J5W3_MARPK
LinkDB: H2J5W3_MARPK
Original site: H2J5W3_MARPK 
ID   H2J5W3_MARPK            Unreviewed;       219 AA.
AC   H2J5W3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   03-APR-2013, entry version 10.
DE   RecName: Full=Probable transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=Marpi_1801;
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Marinitoga.
OX   NCBI_TaxID=443254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC       stage): step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B
CC       subfamily.
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DR   EMBL; CP003257; AEX86182.1; -; Genomic_DNA.
DR   RefSeq; YP_005097480.1; NC_016751.1.
DR   EnsemblBacteria; AEX86182; AEX86182; Marpi_1801.
DR   GeneID; 11604500; -.
DR   KEGG; mpz:Marpi_1801; -.
DR   KO; K00616; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00494; Transaldolase_3b; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; Transaldolase.
DR   InterPro; IPR004731; Transaldolase_3A/3B.
DR   InterPro; IPR022999; Transaldolase_3B.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; Transaldolase; 1.
DR   TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Pentose shunt; Transferase.
FT   ACT_SITE     84     84       By similarity.
SQ   SEQUENCE   219 AA;  24433 MW;  D9F0B3D7B9071C2E CRC64;
     MKIFLDTANI EQIKIAKDWG IIDGVTTNPT LVAKEGNIDF ETRVKEICDV VQGPVSAEVV
     SMDYENMVKE ARELAKISEH VVIKIPMTKD GIKAVKTLSS EGIKTNVTLV FSPLQALLAA
     KAGATYVSPF IGRVDDIGNQ GLELIEEILQ IFYNYGFETE VIAASVRHPY HVVEVAKMGC
     DVATIPFSVL EKLFMHPLTD RGIERFSKDW EEYLKLKNK
//
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