ID   D2QAD8_BIFDB            Unreviewed;       367 AA.
AC   D2QAD8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   OrderedLocusNames=BDP_1144 {ECO:0000313|EMBL:ADB09774.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09774.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB09774.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
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; CP001750; ADB09774.1; -; Genomic_DNA.
DR   RefSeq; WP_003840161.1; NC_013714.1.
DR   AlphaFoldDB; D2QAD8; -.
DR   STRING; 401473.BDP_1144; -.
DR   GeneID; 69536682; -.
DR   KEGG; bde:BDP_1144; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008693; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:ADB09774.1}.
FT   ACT_SITE        138
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   367 AA;  39875 MW;  F3D4B25088BB1E3F CRC64;
     MTEATQRTSD SGVSIWLDDL SRTRIESGNL QELIKDKNVV GVTTNPSIFQ KALSQVGPYD
     AQLKELGKVD VETAIRELTT TDVRNATDIF REVAEATDFV DGRVSIEVDP RLAHETEATE
     KQAVELWEKV NRPNAMIKIP ATLEGLPAIT ATLAKGISVN VTLIFSLERY EQVIDAFIEG
     IAQADANGHD LNHIGSVASF FVSRVDTAVD KQLEEIGSDE AKALEGKAAI ANARLAYELF
     ENKFANDPRW AALEAKGAKK QRPLWASTGT KNPAYSDCVY VDELVAPFIV NTMPEKTLNA
     LADHGNGAPT IKGTYEESHA IMAKLAELGI DFKAVTDKLE ADGVAAFIKS WDSVLTDVQA
     GIDRVNG
//