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Database: UniProt
Entry: A0A172TH57_9BACL
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ID   A0A172TH57_9BACL        Unreviewed;       670 AA.
AC   A0A172TH57;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   ORFNames=SY83_08735 {ECO:0000313|EMBL:ANE46350.1};
OS   Paenibacillus swuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE46350.1, ECO:0000313|Proteomes:UP000076927};
RN   [1] {ECO:0000313|EMBL:ANE46350.1, ECO:0000313|Proteomes:UP000076927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY6 {ECO:0000313|EMBL:ANE46350.1,
RC   ECO:0000313|Proteomes:UP000076927};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP011388; ANE46350.1; -; Genomic_DNA.
DR   RefSeq; WP_068605890.1; NZ_CP011388.1.
DR   AlphaFoldDB; A0A172TH57; -.
DR   STRING; 1178515.SY83_08735; -.
DR   KEGG; pswu:SY83_08735; -.
DR   PATRIC; fig|1178515.4.peg.1744; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000076927; 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:UP000076927};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          17..37
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   670 AA;  72094 MW;  57495C0B452E9148 CRC64;
     MTATNKSIGQ LSIDTIRTLS IDAIEKAKSG HPGMPMGSAP MAYELYSNFM KHNPDQPLWI
     NRDRFVLSAG HGSMLLYSLL HLSGYDLPLE ELKNFRQWGS LTPGHPEWHH TAGVDATTGP
     LGQGIAMAVG MAMAEAQLSA VYNTDKHSVI DHFTYSICGD GDLMEGISSE AASLAGHLKL
     GKLVVLYDSN DISLDGELNL SFSENVAQRF EAYGWHVLRV EDGNDLDALN KAIADARAES
     GKPTLIEVKT VIGYGSPNKG GKGGHAGPHG SPLGVEETKL TKEFYGWTSE EPFFIPEEVK
     GHFAELKSKG INAYEQWTAL VQEYTSANPE LGAQFQAAVN GELPEGWDAE LPRYTTEDKP
     VSTRVASGNA LNGIAKNYPA LVGGSADLES STMTNMKGLP VFTAQNYAGR NIYFGVREFG
     MAAAMNGIML HGGLKVYGGT FFVFTDYLRP AVRLASIMKL PVIYVLTHDS IAVGEDGPTH
     EPIEQLASIR IIPGLTVLRP ADANETSAAW QYAVANKENP VALVLTRQNL PILEGTSDYA
     NLAKGAYVVS DAKAGKPQAQ IIATGSEVQL AVAAQAALAE QGIQVRVISM PSMDLFDKQS
     KEYKDSIILP DVKARLAVEM AHPFGWDRFV GDGGSVLGIE TFGASAPGDR VIKEYGFTVE
     NVVAKVKELL
//
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