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Database: UniProt
Entry: A0A1A2MXG3_9MYCO
LinkDB: A0A1A2MXG3_9MYCO
Original site: A0A1A2MXG3_9MYCO 
ID   A0A1A2MXG3_9MYCO        Unreviewed;       696 AA.
AC   A0A1A2MXG3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN   ORFNames=A5695_02850 {ECO:0000313|EMBL:OBH07579.1};
OS   Mycobacterium sp. E1747.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH07579.1, ECO:0000313|Proteomes:UP000092218};
RN   [1] {ECO:0000313|Proteomes:UP000092218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA   Him V., Kerleguer A., Cheng S.;
RL   Submitted (JUN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBH07579.1}.
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DR   EMBL; LZJI01000181; OBH07579.1; -; Genomic_DNA.
DR   RefSeq; WP_068084412.1; NZ_LZJI01000181.1.
DR   AlphaFoldDB; A0A1A2MXG3; -.
DR   STRING; 1834128.A5695_02850; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000092218; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          31..51
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   696 AA;  75241 MW;  464900ADEB713F59 CRC64;
     MTTLEEISTL TQPHLPDDWS EIDSAAVDTI RVLAADAVQK VGNGHPGTAM SLAPLAYTLF
     QRAMRHDPSD TYWLGRDRFV LSCGHSSLTL YIQLYLGGFG LELSDIESLR TWGSKTPGHP
     EFRHTKGVEI TTGPLGQGLA SAVGMAMASR YERGLFDPDA APGTSPFDHF VYVIASDGDI
     EEGVTSEASS LAAVQQLGNL IVFYDHNQIS IEDDTNIALC EDTAARYEAY GWHVQRVEGG
     ENVVGIEEAI ANAKAVTDRP SFIELRTIIG FPAPKLMNTG KAHGAALGDE EVAAVKEILG
     FDPGKTFEVR DEVIAHTRKL VDRGKEAHEK WQADFDAWAQ REPDRKALLD RLTAEELPDG
     WDADIPTWTT EDKPLATRAA SGKVLNALGP KLPELWGGSA DLAGSNNTTM DNVKSFGPPS
     ISTKDYTADW YGRTLHFGVR EHAMAAILSG IVLHGPTRAY GGTFLQFSDY MRPAVRLAAL
     MDIDTIYVWT HDSIGLGEDG PTHQPIEHLA ALRAIPKLSV VRPADANETA YAWRTILARG
     NGSGPVGLIL TRQGVPILEG TNAEGVARGG YILGDQGTED PDVVLIATGS EVQLAVEAQK
     LLGDKDIAAR VVSMPCVEWF ESQPEDYRDS VLPPSVSARV AVEAGVAQSW HKLVGDTGRI
     VSIEHYGESA DYKTLFREFG FTAEAVAAAA EQVVDN
//
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