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Database: UniProt
Entry: A0A089JNA2_9BACL
LinkDB: A0A089JNA2_9BACL
Original site: A0A089JNA2_9BACL 
ID   A0A089JNA2_9BACL        Unreviewed;       680 AA.
AC   A0A089JNA2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   07-JUN-2017, entry version 20.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   ORFNames=H70737_06125 {ECO:0000313|EMBL:AIQ22459.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22459.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ22459.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22459.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS00651207}.
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DR   EMBL; CP009279; AIQ22459.1; -; Genomic_DNA.
DR   RefSeq; WP_042185576.1; NZ_CP009279.1.
DR   EnsemblBacteria; AIQ22459; AIQ22459; H70737_06125.
DR   KEGG; paej:H70737_06125; -.
DR   KO; K00615; -.
DR   Proteomes; UP000029519; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
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   PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 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   Complete proteome {ECO:0000313|Proteomes:UP000029519};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651241}.
FT   DOMAIN       25     45       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   680 AA;  73340 MW;  621B5112F9FC3AEB CRC64;
     MSEQEQAIQK EENSTVDNLS ITTIRTLAID AIEKANSGHP GMPMGSAPMG YQLFAKTMKH
     NPDHPTWVNR DRFVLSAGHG SMLLYSLLHL SGYDLPMEEL KNFRQWGSLT PGHPEVGHTA
     GVDATTGPLG QGIGMAVGMA MAEAQLGATY NKDEHKVVDH YTYAICGDGD LMEGISSESA
     SLAGHLKLGK LVVLYDSNDI SLDGKLNLSF SENVAQRFDA YGWQVLRVED GNDLPAIAKA
     IAEAQAETSK PTLIEVKTVI GYGSPNKQGK GGHGGTHGSP LGAEEAKLTK DFYKWVYEED
     FYVPDEVRAH FAEVKKNGIA ANKAWDDKFA AYKKAYPELA AQFETVINGD LPEGWDANLP
     TYTTEDKAVS TRVASGSALN GLTAGVPQLV GGSADLESST MTHLNGLTSF TPESYDGRNI
     YFGVREFGMA AAMNGIALHT GLKVFGGTFF VFTDYLRPAI RLASIMKLPV TYVLTHDSIA
     VGEDGPTHEP IEQLASLRII PGLTVIRPAD ANETSAAWAY AMENKENPVA LVLTRQNLPI
     LAGTVDGVRE NIKRGGYVVS DSKNGTPQAQ LIATGSEVQL AVKAQAALAE EGIDVRVISL
     PSWDLFEKQD KEYRDSVILP GVKARLAIEM AQTFGWERYT GDQGDILGIT TFGASAPGDR
     VMKEYGFTVE NVVSRVKALL
//
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