ID G0HDF3_CORVD Unreviewed; 368 AA.
AC G0HDF3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00018292, ECO:0000256|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493,
GN ECO:0000313|EMBL:AEK36827.1};
GN OrderedLocusNames=CVAR_1475 {ECO:0000313|EMBL:AEK36827.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36827.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK36827.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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_00493}.
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_00493};
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_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
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DR EMBL; CP002917; AEK36827.1; -; Genomic_DNA.
DR RefSeq; WP_014009992.1; NC_015859.1.
DR AlphaFoldDB; G0HDF3; -.
DR STRING; 858619.CVAR_1475; -.
DR KEGG; cva:CVAR_1475; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_11; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000006659; Chromosome.
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; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004732; Transaldolase_2.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00876; tal_mycobact; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00493};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:AEK36827.1}.
FT ACT_SITE 143
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 368 AA; 39025 MW; 8A68D50FC1E4C073 CRC64;
MSSSTTPVAD LAAAGTSVWL DDLSRDRITS GNLADLIAGS GVVGVTTNPA IFASAMSKGT
AYDEQIAELK AAGADATEAV FTMAVDDVRN ACGVFADVYR DSAGVDGRVS IEVDPRLAEN
REETVAQAKS LRERVGAENV MIKIPATEVC LPAITEVLGA GISVNVTLIF SVARYRQVID
AFLAGIELAK ANGHDLSTIH SVASFFVSRV DTEIDRRLDE TGGNDALTLK GKAGVANARL
AYEAFNDLLV TGSRWRELAA AGANVQRPLW ASTSVKNPEY SDTLYVTELA GPHTVNTMPE
NTLEATLDHA VITGDTLTGT GEDAAEVFRA LEGVDIDLDD VFRVLEREGV EKFVSSWTDL
LDVIGARL
//
