ID A0A1G4RH09_9CAUL Unreviewed; 217 AA.
AC A0A1G4RH09;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Probable transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00494};
GN ORFNames=SAMN02927928_1930 {ECO:0000313|EMBL:SCW56252.1};
OS Asticcacaulis taihuensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW56252.1, ECO:0000313|Proteomes:UP000199150};
RN [1] {ECO:0000313|EMBL:SCW56252.1, ECO:0000313|Proteomes:UP000199150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW56252.1,
RC ECO:0000313|Proteomes:UP000199150};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_00494}.
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_00494};
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_00494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00494}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000256|ARBA:ARBA00005740, ECO:0000256|HAMAP-Rule:MF_00494}.
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DR EMBL; FMTS01000002; SCW56252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4RH09; -.
DR STRING; 260084.SAMN02927928_1930; -.
DR OrthoDB; 9807051at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000199150; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR NCBIfam; TIGR00875; fsa_talC_mipB; 1.
DR PANTHER; PTHR10683:SF40; FRUCTOSE-6-PHOSPHATE ALDOLASE 1-RELATED; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00494};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00494};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00494};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00494}.
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ SEQUENCE 217 AA; 23095 MW; EB45E3AF90E17E71 CRC64;
MLLFADTADT KILAELLETG LIDGVTTNPT LIAKSGRNIL EVIKEICGMC DGPISAEVAA
TDAATMIKEG EKLAKIASNV VIKVPLTIDG LKATKEFSAQ GLMTNVTLCF SATQALLAAK
AGATYISPFV GRLDDQGADG MQLIHDIRAV YDNYDFDTEI LAASLRNNTH VAQAAIAGAD
CATLPPQTFR DMFKHPLTDK GLETFLSDWK STGQSIL
//