ID A0A2P8QA49_9ACTN Unreviewed; 615 AA.
AC A0A2P8QA49;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:PSM43120.1};
GN ORFNames=C6Y14_13270 {ECO:0000313|EMBL:PSM43120.1};
OS Streptomyces dioscori.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=2109333 {ECO:0000313|EMBL:PSM43120.1, ECO:0000313|Proteomes:UP000240429};
RN [1] {ECO:0000313|EMBL:PSM43120.1, ECO:0000313|Proteomes:UP000240429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A217 {ECO:0000313|EMBL:PSM43120.1,
RC ECO:0000313|Proteomes:UP000240429};
RA Zhikuan W.;
RT "Streptomyces dioscori sp. nov., a novel endophytic actinobacterium
RT isolated from bulbil of Dioscorea bulbifera L.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:PSM43120.1}.
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DR EMBL; PYBJ01000007; PSM43120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8QA49; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000240429; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000240429};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 305..468
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 615 AA; 65494 MW; 5E5AA89132BA5457 CRC64;
MNTPELIELG QQLRVDSVRA AAAAGSGHPT SSMSAADLMA VLLARQLRYD FERPSHPGND
RFVLSKGHAS PLLYAAYKAA GAIDDAELLT FRTLDSRLEG HPTPRRLPWV ETATGSLGQG
LPVGVGIALS GKRLDRVGYR VWVLCGDSEL AEGSIWEAAE HAAYENLDNL TAIVDVNRLG
QRGPTRHGHD LDAYARRFRA FGWHTVEVDG HDVEDIERAY GEAVSTVGQP TVILARTLKG
KGVASVQDRE GLHGKPLPDA DEAIEELGGV RDLRVEVRQP QAARMLHAVR AGHLDLPRWE
TGDEAATRDA YGQALAALGS SRADVVALDG EVSDSTRAEF FAKEHPERFF ECYIAEQQLV
GAAVGLATRG WVPFASSFAA FLTRAHDFVR MAAVSGIGIN LVGSHAGVAI GEDGPSQMGV
EDLAMFRAVH GSTVLYPCDA NQTAALVAGM AGLDGIRYLR TSRGAVPVLY GPGEEFPVGG
SKVLRRSPDD RLTVVAAGVT VHEALKAADA LAADGIAVRV VDLYSVKPVD RETLREAAEQ
TGCLLTVEDH RPEGGIGDAV LDAFLDGRPT PRLVRLAVRD MPGSATPAEQ LRAAGIDAES
VVAAVKLLVE NAVVR
//
