ID A0A3S8WQ03_9ACTN Unreviewed; 615 AA.
AC A0A3S8WQ03;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AZM59001.1};
GN ORFNames=DLM49_04970 {ECO:0000313|EMBL:AZM59001.1};
OS Streptomyces sp. WAC 01438.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM59001.1, ECO:0000313|Proteomes:UP000271045};
RN [1] {ECO:0000313|EMBL:AZM59001.1, ECO:0000313|Proteomes:UP000271045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM59001.1,
RC ECO:0000313|Proteomes:UP000271045};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-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}.
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DR EMBL; CP029601; AZM59001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8WQ03; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000271045; Chromosome.
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:UP000271045};
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"
FT REGION 270..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 65030 MW; C54EFB86AD47D597 CRC64;
MNTGELVELG QQLRVDSVRA AAAAGSGHPT SSMSAADLMA VLFARHLAYD FRQPDAPAND
RFILSKGHAS PLMYATYKAA GAIDDEELLT FRDEGSRLEG HPTPRRLPWV ETATGSLGQG
LPVGVGIALA GKRLDRADYR VWVLCGDSEL AEGSVWEAAE HAAYEHLDNL TLIVDVNRLG
QRGPTRHGHD LDAYARRFQA FGWHTVEVDG HDVDAVDRAY GEAASTKGAP TAILARTLKG
KGVASVQDRE GQHGKPLPEA EEAIAELGGP RDLRLHVRRP SPDGSRPARH GEDPVLPRWD
KGEEVATRNA FGEALTALGT ARGDVVALDG EVGDSTRAEF FAKEHPERYI ECYIAEQQMV
AAAVGVAARG WTPYASTFAA FLTRAHDFIR MASVSGSGIN LVGSHAGVAI GQDGPSQMGL
EDLAMMRAVH GSTVLYPCDA NQTARLVAAM AGLDGIRYLR TSRGGSPVIY GPDEEFPVGG
SKVLRSSGRD RLTLVAAGVT VPEALAAADA LAAEGIAVRV VDLYSVKPVD RATLRTAAEE
TGCLVTVEDH HPEGGLGDAV AEAFADGRPV PRLVRLAVRN MPGSASPDEQ LRASGIDAES
IAAAGRLLVG EAIVS
//
