ID A0A0W1KN12_9ACTO Unreviewed; 366 AA.
AC A0A0W1KN12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:KTF05017.1};
GN ORFNames=AQZ59_00325 {ECO:0000313|EMBL:KTF05017.1};
OS Trueperella bernardiae.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF05017.1, ECO:0000313|Proteomes:UP000054404};
RN [1] {ECO:0000313|EMBL:KTF05017.1, ECO:0000313|Proteomes:UP000054404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF05017.1,
RC ECO:0000313|Proteomes:UP000054404};
RA Bernier A.-M., Bernard K.;
RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT 0504T, Isolated from Blood Culture.";
RL Submitted (NOV-2015) 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}.
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:KTF05017.1}.
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DR EMBL; LNIZ01000001; KTF05017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1KN12; -.
DR STRING; 59561.AQZ59_00325; -.
DR PATRIC; fig|59561.3.peg.320; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000054404; 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 Reference proteome {ECO:0000313|Proteomes:UP000054404};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:KTF05017.1}.
FT ACT_SITE 139
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 366 AA; 39935 MW; 3B90D0E8A74D5D41 CRC64;
MSNLAKLSEL GVSIWLDDLS RSRLDSGNLE DLIRNYNVVG VTTNPSIFQA AISGSDAYRE
DVARLAEAGK TAEEIITELT TDDVRRACDL FAPTFEASRG YDGRVSIEVD PRLAHNPNPT
FAQAKELWAK VDRPNVMIKI PATKAGLPAI RDAIAEGLSV NVTLIFSVER YEEVIDAYLS
GLEAARAAGK DLSTIHSVAS FFVSRVDTEI DARLEKIGGQ SSLDMRGKAG IANARNAYAA
FLKHFESERF RDLEDEGANL QRPLWASTGV KNPDYSPTMY VDQLATTHVV NTMPEATLWA
TKDGAQLDAD TVRPNLDAAS NTMKHLTLLG IDVPGVAAKL EEEGVEKFET AWEELIDTVT
DAMNAN
//
