ID A0A0F4NL05_9VIBR Unreviewed; 316 AA.
AC A0A0F4NL05;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=TW81_05680 {ECO:0000313|EMBL:KJY83817.1};
OS Vibrio galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579748 {ECO:0000313|EMBL:KJY83817.1, ECO:0000313|Proteomes:UP000033673};
RN [1] {ECO:0000313|EMBL:KJY83817.1, ECO:0000313|Proteomes:UP000033673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2757 {ECO:0000313|EMBL:KJY83817.1,
RC ECO:0000313|Proteomes:UP000033673};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY83817.1}.
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DR EMBL; JXXV01000012; KJY83817.1; -; Genomic_DNA.
DR RefSeq; WP_045954740.1; NZ_JXXV01000012.1.
DR AlphaFoldDB; A0A0F4NL05; -.
DR STRING; 579748.TW81_05680; -.
DR PATRIC; fig|579748.3.peg.1160; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000033673; 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:UP000033673};
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 316 AA; 34725 MW; 8456E779166DA2C1 CRC64;
MSNKLEQLRK LTTVVADTGE IDAIKKYQPE DATTNPSLIL KAAQIAEYAP LIDASIEYAK
AQSNNKAQQV QDTCDMLAVN IGKEILKTIP GRISTEVDAR LSYDTQGSVA KARQLVKMYN
DAGITNDRIL IKLASTWEGI RAAEILEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
RIMDWYKAKE GRDFEASEDP GVISVTDIYN YYKEHGYNTV VMGASFRNIG EILELAGCDR
LTIAPALLAE LEAAEGEVVE KLVDSKGSKE RPAPMTHAEF LWEHNLDAMA VEKVAEGIRN
FAVDQGKLED MIAAKL
//
