TAL_NEIG1
ID TAL_NEIG1 Reviewed; 351 AA.
AC Q5F6E9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=NGO1610;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00493}.
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DR EMBL; AE004969; AAW90238.1; -; Genomic_DNA.
DR RefSeq; WP_003689551.1; NC_002946.2.
DR RefSeq; YP_208650.1; NC_002946.2.
DR PDB; 3CLM; X-ray; 1.14 A; A=1-351.
DR PDB; 6ZWF; X-ray; 1.05 A; A=1-351.
DR PDB; 6ZWH; X-ray; 1.50 A; A=1-351.
DR PDB; 6ZWJ; X-ray; 1.35 A; A=1-351.
DR PDB; 6ZX4; X-ray; 0.96 A; A=1-351.
DR PDB; 7B0L; X-ray; 1.65 A; A=1-351.
DR PDB; 7BBW; X-ray; 1.25 A; A/B=2-351.
DR PDB; 7BBX; X-ray; 0.85 A; A=1-351.
DR PDB; 7OEY; X-ray; 1.35 A; A/B=1-351.
DR PDBsum; 3CLM; -.
DR PDBsum; 6ZWF; -.
DR PDBsum; 6ZWH; -.
DR PDBsum; 6ZWJ; -.
DR PDBsum; 6ZX4; -.
DR PDBsum; 7B0L; -.
DR PDBsum; 7BBW; -.
DR PDBsum; 7BBX; -.
DR PDBsum; 7OEY; -.
DR AlphaFoldDB; Q5F6E9; -.
DR SMR; Q5F6E9; -.
DR STRING; 242231.NGO_1610; -.
DR EnsemblBacteria; AAW90238; AAW90238; NGO_1610.
DR GeneID; 66753819; -.
DR KEGG; ngo:NGO_1610; -.
DR PATRIC; fig|242231.10.peg.1924; -.
DR HOGENOM; CLU_050771_1_0_4; -.
DR OMA; ATECYYQ; -.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; Q5F6E9; -.
DR Proteomes; UP000000535; 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; -; 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 PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR TIGRFAMs; TIGR00876; tal_mycobact; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pentose shunt; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1..351
FT /note="Transaldolase"
FT /id="PRO_1000026529"
FT ACT_SITE 138
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:7BBX"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 71..96
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:7BBX"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 221..238
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:7BBX"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:7BBX"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:7BBX"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 324..347
FT /evidence="ECO:0007829|PDB:7BBX"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7BBX"
SQ SEQUENCE 351 AA; 37502 MW; 7278146C5F695095 CRC64;
MTILSDVKAL GQQIWLDNLS RSLVQSGELA QMLKQGVCGV TSNPAIFQKA FAGDALYADE
VAALKRQNLS PKQRYETMAV ADVRAACDVC LAEHESTGGK TGFVSLEVSP ELAKDAQGTV
EEARRLHAAI ARKNAMIKVP ATDAGIDALE TLVSDGISVN LTLLFSRAQT LKAYAAYARG
IAKRLAAGQS VAHIQVVASF FISRVDSALD ATLPDRLKGK TAIALAKAAY QDWEQYFTAP
EFAALEAQGA NRVQLLWAST GVKNPAYPDT LYVDSLIGVH TVNTVPDATL KAFIDHGTAK
ATLTESADEA RARLAEIAAL GIDVETLAAR LQEDGLKQFE EAFEKLLAPL V
