ID U1HUZ9_ENDPU Unreviewed; 342 AA.
AC U1HUZ9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Transaldolase {ECO:0000256|RuleBase:RU000501};
DE EC=2.2.1.2 {ECO:0000256|RuleBase:RU000501};
GN ORFNames=EPUS_09152 {ECO:0000313|EMBL:ERF73134.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73134.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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|RuleBase:RU000501}.
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DR EMBL; KE720974; ERF73134.1; -; Genomic_DNA.
DR RefSeq; XP_007801215.1; XM_007803024.1.
DR AlphaFoldDB; U1HUZ9; -.
DR GeneID; 19243985; -.
DR eggNOG; KOG2772; Eukaryota.
DR HOGENOM; CLU_047470_1_0_1; -.
DR OMA; FEVMAIR; -.
DR OrthoDB; 2716943at2759; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000019373; Unassembled WGS sequence.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF34; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 4: Predicted;
KW Pentose shunt {ECO:0000256|RuleBase:RU000501};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|RuleBase:RU000501}.
SQ SEQUENCE 342 AA; 38335 MW; D559A9F38CE04166 CRC64;
MGSINESERY VNLLEYLRSR TQVDCDSLDI QIVTELGPFV DCTSNQADSY FELLNPRRAA
LLKKSADLSR HILPEYPDVS FEELAVEISM ISLSLTIAPL IPGNIHVMAN PSLSYSTPKV
IQNGQRIASL CQRLDPSFDL SRLCIKVPAT WEGLQACRKL KDLGIKTLAT TLFTMEQAIL
AAEAGCISIS PFVHELRVHF DEEYHDTDPI FDLCVKAQQY FERYSYATRV KACSLISVDE
VMQVAGVAAL TLPPTLLHPL SEMTEPEAKV AALSLFNHNT KIEGQEMERR SFLDEEARFR
ETFAKRDGGK GRVKTTQAID LFCEYQLKAE ALMKDTDTTI VA
//
