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Database: UniProt
Entry: G0ACH9_COLFT
LinkDB: G0ACH9_COLFT
Original site: G0ACH9_COLFT 
ID   G0ACH9_COLFT            Unreviewed;       329 AA.
AC   G0ACH9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=talB2 {ECO:0000313|EMBL:AEK62774.1};
GN   Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=CFU_2948 {ECO:0000313|EMBL:AEK62774.1};
OS   Collimonas fungivorans (strain Ter331).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392};
RN   [1] {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK62774.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA   Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT   "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT   expression of ribosomal RNA genes by large-insert library fluorescent in
RT   situ hybridization (LIL-FISH).";
RL   Environ. Microbiol. 6:990-998(2004).
RN   [2] {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK62774.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA   Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT   "Genomic flank-sequencing of plasposon insertion sites for rapid
RT   identification of functional genes.";
RL   J. Microbiol. Methods 66:276-285(2006).
RN   [3] {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK62774.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA   Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA   Leveau J.H.;
RT   "Identification and characterization of genes underlying chitinolysis in
RT   Collimonas fungivorans Ter331.";
RL   FEMS Microbiol. Ecol. 66:123-135(2008).
RN   [4] {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK62774.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA   Leveau J.H., Uroz S., de Boer W.;
RT   "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT   solutions to life in oligotrophic soil environments.";
RL   Environ. Microbiol. 12:281-292(2010).
RN   [5] {ECO:0000313|EMBL:AEK62774.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK62774.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA   Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA   van den Berg M., Leveau J.H.;
RT   "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT   Collimonas fungivorans versus Aspergillus niger.";
RL   ISME J. 5:1494-1504(2011).
RN   [6] {ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA   Leveau J.H.;
RT   "Complete sequence of Collimonas fungivorans Ter331.";
RL   Submitted (MAY-2011) 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_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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; CP002745; AEK62774.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0ACH9; -.
DR   STRING; 1005048.CFU_2948; -.
DR   KEGG; cfu:CFU_2948; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_4; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008392; 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; 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:UP000008392};
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        134
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   329 AA;  35670 MW;  65A9100012BD4794 CRC64;
     MHSLYTRTDM NQLDQLKQYT TVVADTGNFK QLAQFKPRDA TTNPSLILKA VQQADYAPLL
     VETVAAHADS PLDQIVDQVL VRFGLEILQV VPGRVSTEVD ARLSFDTAAT VARARRIMAL
     YEAAGIGRER VLIKIASTWE GIQAAAILEK DGIRCNLTLL FAFCQAVACG AAKVRLISPF
     VGRIYDWYKK SAGSAWDESA NTLANDPGVK SVAQIYSYYK RFGIATEVMG ASFRNVGQIA
     ALAGCDLLTI SPELLAQLQA SDAPLARALD KDAAAADLQQ VSYDEASFRY ALNDDAMATE
     KLAEGIRGFA ADAFKLDHII EGLLASIRA
//
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