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Database: UniProt
Entry: A0A1M5LRE8_9ALTE
LinkDB: A0A1M5LRE8_9ALTE
Original site: A0A1M5LRE8_9ALTE 
ID   A0A1M5LRE8_9ALTE        Unreviewed;       320 AA.
AC   A0A1M5LRE8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN   ORFNames=SAMN05216361_2759 {ECO:0000313|EMBL:SHG67546.1};
OS   Marisediminitalea aggregata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marisediminitalea.
OX   NCBI_TaxID=634436 {ECO:0000313|EMBL:SHG67546.1, ECO:0000313|Proteomes:UP000184520};
RN   [1] {ECO:0000313|Proteomes:UP000184520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8995 {ECO:0000313|Proteomes:UP000184520};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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|ARBA:ARBA00003518,
CC       ECO:0000256|HAMAP-Rule:MF_00492, ECO:0000256|RuleBase:RU004155}.
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_00492, ECO:0000256|RuleBase:RU004155};
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_00492, ECO:0000256|RuleBase:RU004155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|HAMAP-Rule:MF_00492,
CC       ECO:0000256|RuleBase:RU004155}.
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DR   EMBL; FQWD01000004; SHG67546.1; -; Genomic_DNA.
DR   RefSeq; WP_073323400.1; NZ_JANDJN010000021.1.
DR   AlphaFoldDB; A0A1M5LRE8; -.
DR   STRING; 634436.SAMN05216361_2759; -.
DR   OrthoDB; 9809101at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000184520; 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; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW   Rule:MF_00492}; Reference proteome {ECO:0000313|Proteomes:UP000184520};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00492};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00492}.
FT   ACT_SITE        132
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   320 AA;  34588 MW;  D1B8C7D0C8A4AA24 CRC64;
     MSNQLASLRK ITTVVADTGD IEAIKKYQPV DATTNPSLLL KAAGMPQYAS LIDDAVAWAA
     EQSSDPAQQL TDAADKLAVS IGKEISATIP GRISTEVDAR LSFDTEATIA KAERLVQLYA
     DAGIDKSRIL IKIASTWEGI KAAEVLEKQG VNCNLTLLFS FAQARACAEA GVFLISPFVG
     RILDWYKKST GKDSYEASED PGVVSVTNIY NFYKANGYNT IVMGASFRNT GEILELAGCD
     RLTISPNLLE ELANTDGEVE AKLVDNGATE APGERLDESG FRWEMNEDAM ATEKLAEGIR
     NFAADQDKLE TMLKDKLANL
//
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