ID A0A255GFK5_9ACTN Unreviewed; 369 AA.
AC A0A255GFK5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, 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:OYO14627.1};
GN ORFNames=CGZ94_08615 {ECO:0000313|EMBL:OYO14627.1};
OS Enemella evansiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016499 {ECO:0000313|EMBL:OYO14627.1, ECO:0000313|Proteomes:UP000215896};
RN [1] {ECO:0000313|EMBL:OYO14627.1, ECO:0000313|Proteomes:UP000215896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 030167 {ECO:0000313|EMBL:OYO14627.1,
RC ECO:0000313|Proteomes:UP000215896};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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_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}.
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:OYO14627.1}.
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DR EMBL; NMVO01000012; OYO14627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255GFK5; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000215896; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000215896};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 140
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 369 AA; 39616 MW; CB7552573AB211A4 CRC64;
MSDRLKKLSD AGVSIWLDDL SRERIATGDL AKLVTESSVV GVTTNPTIFA TALSNGEAYE
AQLQILRDRG TGVDEAIQAL TTDDVRAACD VLSATNRATD KVDGRVSIEV EPGLARDTAG
TIAQAKQLAE VVGRDNVLIK IPATEEGLPA ITATIAEGIS VNVTLIFSLE RYQGVMDAYL
AGLEQAAEQG RDLSRLHSVA SFFVSRVDSE VDKRLDAIGT EQATQLKGKA AVANARLAYE
LYQQVFESGE RFAALKAKGA TVQRPLWAST GVKDPAYPDT LYVAELIAPG TVNTMPEKTM
QAFADHGEVT ADAITPNLDD ARQTMAALEQ VGIDLDDVVR VLEDEGVEKF DKSWAELVET
VTDQLKQSS
//
