TAL_BACSU
ID TAL_BACSU Reviewed; 212 AA.
AC P19669;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
DE AltName: Full=20 kDa phosphoprotein OrfU;
DE AltName: Full=CSI9;
GN Name=tal; Synonyms=ywjH; OrderedLocusNames=BSU37110;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=2457578; DOI=10.1128/jb.170.9.4194-4208.1988;
RA Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.;
RT "Complete sequence and transcriptional analysis of the spo0F region of the
RT Bacillus subtilis chromosome.";
RL J. Bacteriol. 170:4194-4208(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [5]
RP SEQUENCE REVISION TO 100.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP PROTEIN SEQUENCE OF 1-24, AND PHOSPHORYLATION.
RX PubMed=1556067; DOI=10.1128/jb.174.8.2474-2477.1992;
RA Mitchell C., Morris P.W., Vary J.C.;
RT "Identification of proteins phosphorylated by ATP during sporulation of
RT Bacillus subtilis.";
RL J. Bacteriol. 174:2474-2477(1992).
RN [7]
RP PROTEIN SEQUENCE OF 1-15.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11120740; DOI=10.1074/jbc.m008061200;
RA Schuermann M., Sprenger G.A.;
RT "Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia
RT coli and is related to a novel group of bacterial transaldolases.";
RL J. Biol. Chem. 276:11055-11061(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. Does not show fructose-6-P aldolase
CC activity. {ECO:0000269|PubMed:11120740}.
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:0000269|PubMed:11120740};
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.
CC -!- INTERACTION:
CC P19669; P19669: tal; NbExp=2; IntAct=EBI-7631043, EBI-7631043;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89874.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M22039; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M22039; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; Z49782; CAA89874.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB15728.3; -; Genomic_DNA.
DR PIR; F32354; F32354.
DR RefSeq; NP_391592.3; NC_000964.3.
DR RefSeq; WP_003227626.1; NZ_JNCM01000034.1.
DR PDB; 3R8R; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/R/T/U/V/W=1-212.
DR PDBsum; 3R8R; -.
DR AlphaFoldDB; P19669; -.
DR SMR; P19669; -.
DR IntAct; P19669; 1.
DR MINT; P19669; -.
DR STRING; 224308.BSU37110; -.
DR iPTMnet; P19669; -.
DR jPOST; P19669; -.
DR PaxDb; P19669; -.
DR PRIDE; P19669; -.
DR EnsemblBacteria; CAB15728; CAB15728; BSU_37110.
DR GeneID; 938462; -.
DR KEGG; bsu:BSU37110; -.
DR PATRIC; fig|224308.179.peg.4020; -.
DR eggNOG; COG0176; Bacteria.
DR InParanoid; P19669; -.
DR OMA; VRHPMHV; -.
DR PhylomeDB; P19669; -.
DR BioCyc; BSUB:BSU37110-MON; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Pentose shunt;
KW Phosphoprotein; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..212
FT /note="Transaldolase"
FT /id="PRO_0000173658"
FT ACT_SITE 84
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 100
FT /note="D -> G (in Ref. 1; M22039 and 2; CAA89874)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3R8R"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:3R8R"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:3R8R"
SQ SEQUENCE 212 AA; 22971 MW; 59EA1748FB2CBCD6 CRC64;
MLFFVDTANI DEIREANELG ILAGVTTNPS LVAKEANVSF HDRLREITDV VKGSVSAEVI
SLKAEEMIEE GKELAKIAPN ITVKIPMTSD GLKAVRALTD LGIKTNVTLI FNANQALLAA
RAGATYVSPF LGRLDDIGHN GLDLISEVKQ IFDIHGLDTQ IIAASIRHPQ HVTEAALRGA
HIGTMPLKVI HALTKHPLTD KGIEQFLADW NK
