ID A0A1Z4LVS1_9CYAN Unreviewed; 383 AA.
AC A0A1Z4LVS1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=NIES267_48550 {ECO:0000313|EMBL:BAY85355.1};
OS Calothrix parasitica NIES-267.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1973488 {ECO:0000313|EMBL:BAY85355.1, ECO:0000313|Proteomes:UP000218418};
RN [1] {ECO:0000313|EMBL:BAY85355.1, ECO:0000313|Proteomes:UP000218418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-267 {ECO:0000313|EMBL:BAY85355.1,
RC ECO:0000313|Proteomes:UP000218418};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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; AP018227; BAY85355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4LVS1; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000218418; 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.
DR PROSITE; PS00958; TRANSALDOLASE_2; 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}.
FT ACT_SITE 143
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 383 AA; 42504 MW; DED97ABBDECF6BA1 CRC64;
MGITTNQLLE INKYGQSIWM DNLSRDLIQS GELKNMVENQ GIKGITSNPS IFEKAIAGNA
IYDKDIEAAI NKGLSTQDIY ESLAFEDIRN ACDILKPVYE ATDGLDGYVS IEVPPTIAND
TQKTIEEARR YFKEVGRENL MIKIPGTEAG LPAVEQVISE GMNVNITLLF SVDSYVNTAW
AYIRGLEKRV AEGKDISKIS SVASFFLSRI DSKIDGKIDD KLAQGVDDIN LEAKLKSVKG
KVAIANAKIA YQEYKKIIND KRWQALTEKG AKVQRLLWAS TSTKDPSYSD VMYVDELIGK
ETVNTLPPVT IEACADHCDV ESRVETDVEA AYKVIESLKD PDINIDLDTV MDELLTEGID
KFIKPFQSLI SSLEDKVKQL SPV
//
