ID M3AZX0_SPHMS Unreviewed; 324 AA.
AC M3AZX0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
GN ORFNames=SEPMUDRAFT_148448 {ECO:0000313|EMBL:EMF13077.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF13077.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF13077.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF13077.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the non-oxidative phase
CC in the pentose phosphate pathway. Catalyzes the reversible conversion
CC of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC erythrose-4-phosphate and beta-D-fructose 6-phosphate.
CC {ECO:0000256|RuleBase:RU000501}.
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|RuleBase:RU000501};
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,
CC ECO:0000256|RuleBase:RU000501}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012}.
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DR EMBL; KB456263; EMF13077.1; -; Genomic_DNA.
DR RefSeq; XP_016761198.1; XM_016904937.1.
DR AlphaFoldDB; M3AZX0; -.
DR STRING; 692275.M3AZX0; -.
DR GeneID; 27902074; -.
DR eggNOG; KOG2772; Eukaryota.
DR HOGENOM; CLU_047470_0_1_1; -.
DR OMA; FATIKKY; -.
DR OrthoDB; 1972468at2759; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00874; talAB; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF18; 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 Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000501};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000501}.
SQ SEQUENCE 324 AA; 35525 MW; FF3D8F779B37137B CRC64;
MTSSLDQLKA TGTTVVCDSG DFATIGKYKP QDATTNPSLI LAASKKPEYA KLIDEAVAYG
KKHGKSIDEQ VDATLDNLLV QFGKEILNIV PGKVSTEVDA RFSFDKKASV DKALHLIELY
KAEGIDKSRV LIKLASTWEG IQAAHELQSK HGINCNLTLM FSLPQAIAAA EAGAFLISPF
VGRILDWYKA NTKQEYTPEN DPGVKSVQQI FNYYKKFGYK TIVMGASFRS VGEVTELAGC
DYLTIAPNLL EQLYNSTDAV PKKLESESAA SLNIEKKSYL ANEGDFRFDF NEDTMAVHKL
SEGISKFAAD AVTLKDILKQ KINA
//
