ID A1VVU0_POLNA Unreviewed; 368 AA. AC A1VVU0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 10-MAY-2017, entry version 76. DE RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670}; DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670}; GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493}; GN OrderedLocusNames=Pnap_4495 {ECO:0000313|EMBL:ABM39768.1}; OS Polaromonas naphthalenivorans (strain CJ2). OG Plasmid pPNAP02 {ECO:0000313|EMBL:ABM39768.1, OG ECO:0000313|Proteomes:UP000000644}. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM39768.1, ECO:0000313|Proteomes:UP000000644}; RN [1] {ECO:0000313|Proteomes:UP000000644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644}; RC PLASMID=Plasmid pPNAP02 {ECO:0000313|Proteomes:UP000000644}; RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x; RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.; RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from RT coal tar-contaminated sediment, reveals physiological and metabolic RT versatility and evolution through extensive horizontal gene RT transfer."; RL Environ. Microbiol. 11:2253-2270(2009). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. {ECO:0000256|HAMAP- CC Rule:MF_00493}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118662}. 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. {ECO:0000256|HAMAP-Rule:MF_00493, CC ECO:0000256|SAAS:SAAS00118684}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493, CC ECO:0000256|SAAS:SAAS00399167}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00493}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000531; ABM39768.1; -; Genomic_DNA. DR RefSeq; WP_011798197.1; NC_008758.1. DR RefSeq; WP_011798197.1; NC_008758.1. DR RefSeq; WP_011798197.1; NC_008758.1. DR ProteinModelPortal; A1VVU0; -. DR EnsemblBacteria; ABM39768; ABM39768; Pnap_4495. DR KEGG; pna:Pnap_4495; -. DR PATRIC; 22943524; VBIPolNap76733_0339. DR HOGENOM; HOG000226074; -. DR KO; K00616; -. DR OMA; WLDNITR; -. DR OrthoDB; POG091H05PS; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000000644; Plasmid pPNAP02. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR CDD; cd00955; Transaldolase_like; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00493; Transaldolase_2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR004732; Transaldolase_2. DR PANTHER; PTHR10683; PTHR10683; 1. DR PANTHER; PTHR10683:SF21; PTHR10683:SF21; 1. DR Pfam; PF00923; TAL_FSA; 1. DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1. DR TIGRFAMs; TIGR00876; tal_mycobact; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493, KW ECO:0000256|SAAS:SAAS00118680}; KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493, KW ECO:0000256|SAAS:SAAS00118654}; KW Plasmid {ECO:0000313|EMBL:ABM39768.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000644}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493, KW ECO:0000256|SAAS:SAAS00118695}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, KW ECO:0000256|SAAS:SAAS00118651, ECO:0000313|EMBL:ABM39768.1}. FT ACT_SITE 139 139 Schiff-base intermediate with substrate. FT {ECO:0000256|HAMAP-Rule:MF_00493}. SQ SEQUENCE 368 AA; 39006 MW; A0B1330571FB6610 CRC64; MKSTRQLHDL GQSLWLDNIT RTLLDDGTLA RYIAEDSITG LTSNPSIFDA AIGGGEAYDA AIHAKTLAGL AGEALFTELA LEDLRRAADL FRPVFDATDQ ADGWVSMEVS PLLAVDTAGS IAAARQIHDQ AQRANLFVKI PGTPQGIAAI EQAIFLGIPI NVTLLFSCAH YQAAAEAYLR GIERRLAAGL DLRVGSVASL FISRWDVAGN AQLPTELQHK LGIAVARQTY RAYRDLLAST RWQKLAAAGA KPQRLLWAST GTKDPAAPDT LYVSALAAPD TINTLPEKTL HAFADHGRLQ GVMPADGGDA EAVLAQITGA GVDVPTLAAK LQQDGAQSFV KSWQQLMQRI AEKSGALKPA PPASAIGT //