ID   A0A101N307_9ACTN        Unreviewed;       615 AA.
AC   A0A101N307;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:KUM85617.1};
GN   ORFNames=AQI94_27615 {ECO:0000313|EMBL:KUM85617.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM85617.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM85617.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM85617.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
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:KUM85617.1}.
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DR   EMBL; LMWM01000029; KUM85617.1; -; Genomic_DNA.
DR   RefSeq; WP_031043239.1; NZ_KQ948149.1.
DR   AlphaFoldDB; A0A101N307; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000053039; 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   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;  65923 MW;  2EA556FA5F2B22D2 CRC64;
     MNTGELVELA QQLRVDSVRA SAAAGSGHPT SSMSAADLMA VLLANHFRYD FDRPAHPGND
     RFVLSKGHAS PLLYSAYKAA GVVDDEELLT FRKLDSRLEG HPTPRKLPWV ETATGSLGQG
     LPVGVGIALS GKRLDRADYR VWVLCGDSEL AEGSIWEAAE HAGHEHLDNL TAIVDVNRLG
     QRGPTRHGHD LDAYARRFQA FGWHTVEVDG HDVDAIDRAY GEAESTKGQP TAILARTLKG
     KGVADVEDRE GLHGKPLKNA DDAIEELGGV RDLRVRVNEP PAARVLHAVR AGHVELPRWD
     TGEEVATRDA YGQALAALGT GRGDVVALDG EVGDSTRTEY FAKEHADRYF ECYIAEQQMV
     AAAVGLAARG WVPYAGTFAA FLTRAYDFVR MASISGAGLN LVGSHAGVAI GQDGPSQMGL
     EDLAMMRAIH GSTVLYPCDA NQTARLIAEM ADLDGIRYLR TGRGESPVIY GADEQFPIGG
     SKVLRFSQSD RLTVVAAGVT VHEALKAAEA LDQEGIRVRV IDLYSVKPVD RDTLRQAAED
     TGCLLTVEDH REEGGLGDAV LDAFTDGRPV PRPVRLAVRT MPGSASPEEQ LHAAGIDAES
     IGAAVRLLVE QAIVP
//