TAL_PROM9
ID TAL_PROM9 Reviewed; 333 AA.
AC Q31C15;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=PMT9312_0519;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) 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_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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00492}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR EMBL; CP000111; ABB49580.1; -; Genomic_DNA.
DR RefSeq; WP_011376078.1; NC_007577.1.
DR PDB; 3HJZ; X-ray; 1.90 A; A=1-333.
DR PDBsum; 3HJZ; -.
DR AlphaFoldDB; Q31C15; -.
DR SMR; Q31C15; -.
DR STRING; 74546.PMT9312_0519; -.
DR PRIDE; Q31C15; -.
DR EnsemblBacteria; ABB49580; ABB49580; PMT9312_0519.
DR KEGG; pmi:PMT9312_0519; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_3; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; Q31C15; -.
DR Proteomes; UP000002715; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
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; -; 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 PANTHER; PTHR10683; PTHR10683; 1.
DR PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00874; talAB; 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; Schiff base; Transferase.
FT CHAIN 1..333
FT /note="Transaldolase"
FT /id="PRO_0000230959"
FT ACT_SITE 135
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3HJZ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:3HJZ"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:3HJZ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:3HJZ"
FT HELIX 293..330
FT /evidence="ECO:0007829|PDB:3HJZ"
SQ SEQUENCE 333 AA; 37289 MW; E2EA6FCE1D49C0A4 CRC64;
MKSILEQLSS MTVVVADTGD LDSIKKFQPR DATTNPSLIL AAAKNPDYVK LIDKAIESSE
NTLPNGFSEI ELIKETVDQV SVFFGKEILK IISGRVSTEV DARLSFDTEA TVKKARKLIN
LYKNFGIEKE RILIKIAATW EGIKAAEILE KEGIKCNLTL LFNFCQAVTC ANANITLISP
FVGRILDWHK AKTGKTSFIG AEDPGVISVT QIYKYFKEKG FKTEVMGASF RNLDEIKELA
GCDLLTIAPK FLEELKREKG VLIRKLDAST KINNSIDYKF EEKDFRLSML EDQMASEKLS
EGITGFSKAI EELEELLIER LSEMKNHKLI SAN
