GenomeNet

Database: UniProt
Entry: E3EDN3_PAEPS
LinkDB: E3EDN3_PAEPS
Original site: E3EDN3_PAEPS 
ID   E3EDN3_PAEPS            Unreviewed;       681 AA.
AC   E3EDN3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662, ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN   Name=tktA {ECO:0000313|EMBL:ADO55341.1};
GN   ORFNames=PPSC2_06555 {ECO:0000313|EMBL:ADO55341.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO55341.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO55341.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO55341.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC       ketose donor to an aldose acceptor, via a covalent intermediate with
CC       the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027,
CC         ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC       metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002213; ADO55341.1; -; Genomic_DNA.
DR   RefSeq; WP_013369972.1; NC_014622.2.
DR   AlphaFoldDB; E3EDN3; -.
DR   STRING; 1406.LK13_19520; -.
DR   KEGG; ppm:PPSC2_06555; -.
DR   PATRIC; fig|886882.15.peg.1350; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_9; -.
DR   OMA; GCAPMGY; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000006868; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          25..45
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   681 AA;  73952 MW;  ADA34C83B0E499DF CRC64;
     MTDQNQAIQK DENSTIDNLS ITTIRTLAID AIEKANSGHP GMPMGSAPMG YQLFAKTMNH
     NPDRPTWVNR DRFVLSAGHG SMLLYSLLHL SGYDLPMEEL KQFRQWGSLT PGHPEFGHTA
     GVDATTGPLG QGLAMSVGMA MAEAQLGATY NKDEFKVVDH FTYAICGDGD LMEGISHEAA
     SLAGRLQLGK LIVLFDSNDI TLDGKLNLSS SESVAKRFEA YNWQVLRVED GNDLPAIQKA
     IEEAQADSTR PTLIEVKTVI GYGSPNKQGK GGHGGTHGSP LGAEEAKLTK EFYKWVYEED
     FHVPQEVREH FAKVKERGIA ANKAWDEQFA KYKAAHPDLA AQFETAVNGD LPEGWDRDLP
     KYSTEDKAVS TRVASGNALN GLAPNVPFLT GGSADLESST MTHLNNLTNF TPEDYAGRNI
     YFGIREFGMA AAMNGMALHQ GVKVFGGTFF VFTDYLRPAV RLAALMGLPV TYVLTHDSIA
     VGEDGPTHEP IEQLASLRII PNLTVIRPAD GNETSAAWAY TLENKKNPVA LVLTRQNLPI
     LAATAEHARE GIKRGAYVVA DAADGKPVAQ ILATGSEVQL AVKAQEALAE QGIQVRVISF
     PSWDLFEKQD KAYKDSVLLP EVKARLAVEM AYPLGWEKYV GDQGDILGIS TFGASAPGDR
     VIKEYGFTVE NVVSRVKALL K
//
DBGET integrated database retrieval system