ID C9E301_9BIFI Unreviewed; 162 AA.
AC C9E301;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=transaldolase {ECO:0000256|ARBA:ARBA00013151};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151};
DE Flags: Fragment;
OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=547043 {ECO:0000313|EMBL:ACV83796.1};
RN [1] {ECO:0000313|EMBL:ACV83796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 1200 {ECO:0000313|EMBL:ACV83796.1};
RA Voronina O.L., Kunda M.S., Bitkina V.V., Zhilenkova O.G., Amerkhanova A.M.;
RT "Strains of Bifidobacterium adolescentis group genomic polymorphism.
RT Analysis of collection and infants strains.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518}.
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}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426}.
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DR EMBL; GQ452830; ACV83796.1; -; Genomic_DNA.
DR AlphaFoldDB; C9E301; -.
DR UniPathway; UPA00115; UER00414.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV83796.1"
FT NON_TER 162
FT /evidence="ECO:0000313|EMBL:ACV83796.1"
SQ SEQUENCE 162 AA; 17399 MW; 9470BA2A8F2D403E CRC64;
EGIAQADANG HDLKHIGSVA SFFVSRVDTA VDNKLEEIGS DEAKALEGKA AIANARLAYE
LFENKFANDP RWAALEAKGA KKQRPLWAST GTKNPAYSDC VYVDELVAPL IVNTMPEKTL
NALADHGNGA PTIKGTYEES HAIMAKLAEL GIDFKAVTDK LE
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