ID A0A154QZX5_9GAMM Unreviewed; 364 AA.
AC A0A154QZX5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=RhoFW510R10_01105 {ECO:0000313|EMBL:KZC30776.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC30776.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC30776.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC30776.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
CC ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00493};
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 stage):
CC step 2/3. {ECO:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC Rule:MF_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZC30776.1}.
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DR EMBL; LVJU01000081; KZC30776.1; -; Genomic_DNA.
DR RefSeq; WP_068094961.1; NZ_LVJU01000081.1.
DR AlphaFoldDB; A0A154QZX5; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000076310; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004732; Transaldolase_2.
DR NCBIfam; TIGR00876; tal_mycobact; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 139
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 364 AA; 38918 MW; 408C8C9B5208CF01 CRC64;
MKATRQLHDL GQSLWLDNIT RSLLDDGTLA RYIAEDSITG LTSNPSIFDA AIGGGDAYDA
GIHAKTLAGL SGEALFTELA LEDLRRAADL FRPVFDATRQ VDGWVSMEVS PLLAADTAGS
IAAARHIHHQ GRRDNLFVKI PGTPEGVPAI EEAIFLGIPI NVTLLFSCAQ YQAVAEAYLR
GIERRLEAGL DPRVGSVASL FISRWDVAAN PQLPADLHNR LGIAVGQQTY RAYRELLASK
RWQKLAAAGA QPQRLLWAST GVKDPSAPDT LYVSALAAPD TIDTIPEKTL HAFADHGQLH
GVLAADGGDA DAVLAQVAKA GVDLDALALK LQQDGAAAFV KSWQQLLQRI ADKASALEKE
SELP
//
