ID A0A0X3V9J6_9ACTN Unreviewed; 615 AA.
AC A0A0X3V9J6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KUL39956.1};
GN ORFNames=ADL12_14225 {ECO:0000313|EMBL:KUL39956.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL39956.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUL39956.1}.
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DR EMBL; LLZG01000088; KUL39956.1; -; Genomic_DNA.
DR RefSeq; WP_062702250.1; NZ_LLZG01000088.1.
DR AlphaFoldDB; A0A0X3V9J6; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000053923; 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:UP000053923};
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; 65365 MW; A5CE0E50DF7CB435 CRC64;
MNTAELVELA QQLRVDSVRA SAAAGSGHPT SSMSAADLTA VLLANHLRYD FDRPAHPGND
RFVLSKGHAS PLLYSAYKAA GAIEDGELLT FRKIGSRLEG HPTPRRLPWL ETATGSLGQG
LPIGVGIALA GKRLDRAGYR VWVLCGDSEL AEGSVWEAAE HAAYEHLDNL TAVVDVNRLG
QRGPTRHGHD LHAYARRFQA FGWHTVEVDG HDVDAIDRAY GEARSTSGQP TVILARTLKG
KGVQSVQDRE GLHGKPLPDP DEAIAELGGP RDIHVRVHEP PAARMLHAVP AGHLELPRWE
KGEEVATRNA YGEALAALGT GRGDVVALDG EVSDSTRAEF FAKAHPDRFF ECYIAEQQLV
AAAVGLATRG WVPYASTFAA FLTRAHDFVR MASVSGVGIN LVGSHAGVAI GQDGPSQMGL
EDLAMMRAVH GSTVLYPCDA NQTAKLVAAM ADLDGVRYLR TSRGAAPVVY GPDEEFPVGG
SKVLRSSPYD RLTVVAAGAT VHEALAAADA LDRDGIQVRV VDLYSVKPVD RATLRRAAED
TGCLMTVEDH HEEGGIGDAV LDAFVDGRPV PRLVRLAVRT MPGSASPDEQ LHAAGIDAAC
IAAAGKLLVE EAVVR
//
