ID B7RZ14_9GAMM Unreviewed; 307 AA.
AC B7RZ14;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 ECO:0000313|EMBL:EEB78438.1};
GN ORFNames=GPB2148_155 {ECO:0000313|EMBL:EEB78438.1};
OS marine gamma proteobacterium HTCC2148.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB78438.1, ECO:0000313|Proteomes:UP000002793};
RN [1] {ECO:0000313|Proteomes:UP000002793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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}.
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};
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}.
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}.
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DR EMBL; DS999228; EEB78438.1; -; Genomic_DNA.
DR AlphaFoldDB; B7RZ14; -.
DR STRING; 247634.GPB2148_155; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_6; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000002793; 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.
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:UP000002793};
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 122
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ SEQUENCE 307 AA; 33489 MW; A2868C6C685530FE CRC64;
MTDVVADTGD VEAIGRFQPL DATTNPSLLL KAAALPHYAQ LLDNAKSWAS TEGGSNSEQL
SNSCDHFAVD VGKEILRIIP GRISTEVDAR LSFDTAATMK RARKLIDMYE EAGIGRERIL
IKTASTWEGI RAAAQLEKEG INCNLTLLFG FGQAAACADA GVFLISPFVG RILDWHKANT
DLQIVTPQDD PGVQSVSRIY NYYKQHGYQT IVMGASFRNT GEIESLAGCD RLTISPALLE
ELAADEGDLP RQLEPDGATT SVAKHSPQEH DFRYDLNADA MTTEKLAEGI RSFIGDQIKL
EQLISDR
//
