ID M9M4L9_GLUTH Unreviewed; 956 AA.
AC M9M4L9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=NBRC3255_1027 {ECO:0000313|EMBL:GAC87366.1};
OS Gluconobacter thailandicus NBRC 3255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1291534 {ECO:0000313|EMBL:GAC87366.1, ECO:0000313|Proteomes:UP000011890};
RN [1] {ECO:0000313|Proteomes:UP000011890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3255 {ECO:0000313|Proteomes:UP000011890};
RX PubMed=23580707; DOI=10.1128/genomeA.00118-13;
RA Matsutani M., Kawajiri E., Yakushi T., Adachi O., Matsushita K.;
RT "Draft Genome Sequence of Dihydroxyacetone-Producing Gluconobacter
RT thailandicus Strain NBRC 3255.";
RL Genome Announc. 1:e0011813-e0011813(2013).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
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 GPI family. {ECO:0000256|RuleBase:RU000612}.
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:GAC87366.1}.
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DR EMBL; BAON01000006; GAC87366.1; -; Genomic_DNA.
DR RefSeq; WP_007282544.1; NZ_BAON01000006.1.
DR AlphaFoldDB; M9M4L9; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000011890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
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; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
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; PF00342; PGI; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 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 Gluconeogenesis {ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|RuleBase:RU000612, ECO:0000313|EMBL:GAC87366.1};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00493}; Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 153
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 956 AA; 103311 MW; 36DDA65B28FDFA21 CRC64;
MADTISNTGL EKVGSVLRDL EKHGQSPWLD FIQRSFTEDG SLKKLVEEDG LRGVTSNPAI
FEKAIGKGTE YDPQIRKLLE GEGLSAGDLY EHLAIDDIRA ACGVLYPVFE KTKGLDGYVS
LEVSPYLAFD AHGTITEARR LWKAVGRKNL MVKIPGTAEG TGAIREAIAD GININVTLLF
SLEAYKDVLE AYISGLEARA ARGEDISHIS SVASFFVSRI DAKIDGEIDR RVAAGDKDAE
ALKALRGKVA IANAKVAYQY YLDVKKSPRW QALAAKGANP QRLLWASTGT KDKAYSDVLY
VEELIGPETV NTIPPATFDA FRDHGKLRES LTENVEEARH VLAEAERLGL DLAGVTAKLV
KDGCASFSES FDTLLGAVAE KRESVLGKRL LHVTADLPSE IRDDVAESEK AWSKEGLVRR
IWAKDASVWT NGPEAGWLNW LTIVQDRLWH IEELELLARD VRSRGFTDIL LLGMGGSSLG
PEVLAETFGQ QEGWPKLHVL DSTDPQQVRT YEKAVDLKKT LFIVASKSGG TLEPNILFAH
FWTVAGQALG KAPGDNFIAI TDPDSHMQKV AEENGFWRIF YGDPKIGGRF SVLSNFGLVP
AAVSGLDVRR FLTITTLMVE SCGPSAPAHV NPGVTLGLIL GHSAKCFGRD KVTILASKGI
ASFGAWLEQL IAESTGKKGT GLVPIDEEEL GTPDVYGKDR VFVDLLLEGD TPDSRLGALR
EAGAPVVTVR LSDKNEIGQA FFVFEFATAV AGAVLGIDPF DQPDVEFSKV ETRKLTTAYA
ETGALPAEAP FAVDGNLAFY ADEKNAAALG TGDTVSILKK HFERVGPGDY VGLLAYIERN
RETRDWAQDV RMDLRNALKV ATAAEFGPRF LHSTGQAYKG GPDSGVFLQV TAKDAADVPV
PGHGFSFGVV KAAQARGDFE VLSARGRRAL RVHIDGPLEE GLKTLAGAIH KAIAGA
//
