ID E4V9W0_BIFBI Unreviewed; 367 AA.
AC E4V9W0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 ECO:0000313|EMBL:EFR50402.1};
GN ORFNames=BBNG_00950 {ECO:0000313|EMBL:EFR50402.1};
OS Bifidobacterium bifidum NCIMB 41171.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=398513 {ECO:0000313|EMBL:EFR50402.1, ECO:0000313|Proteomes:UP000002776};
RN [1] {ECO:0000313|EMBL:EFR50402.1, ECO:0000313|Proteomes:UP000002776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 41171 {ECO:0000313|EMBL:EFR50402.1,
RC ECO:0000313|Proteomes:UP000002776};
RG The Broad Institute Genome Sequencing Platform;
RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., Jaffe D.,
RA Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171.";
RL Submitted (AUG-2008) 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 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|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; DS990229; EFR50402.1; -; Genomic_DNA.
DR RefSeq; WP_003813255.1; NZ_DS990229.1.
DR AlphaFoldDB; E4V9W0; -.
DR GeneID; 56627447; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_11; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000002776; 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 InterPro; IPR018225; Transaldolase_AS.
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.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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, ECO:0000313|EMBL:EFR50402.1}.
FT ACT_SITE 138
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 367 AA; 39764 MW; 308C86D3EE7961FE CRC64;
MTEATQRTSD NGVSIWLDDL SRTRIESGSL QELIKDKNVV GVTTNPSIFQ KALSQVGPYD
AQLKELGKVD VETAVRELTT TDVRNATDIF REIAEATDFV DGRVSIEVDP RLAHDTENTE
KQAVELWEKV NRPNAMIKIP ATLEGLPAIT ATLAKGISVN VTLIFSLERY EQVIDAYIEG
IAQAAANGHD LKHIGSVASF FVSRVDTAVD KLLEANGSDE AKALEGKAAV ANARLAYELF
EKKFAADPRW ADLAAKGAKV QRPLWASTGT KNAAYSDCKY VDELVAKHIV NTMPEKTLNA
LADHGNGAPS IEGTYEESHA VIDKLAELGI NLKDVTDKLE ADGVAAFIKS WDSVLADVQS
GIDRVNA
//
