ID A0A1G8ZUT1_9ACTN Unreviewed; 607 AA.
AC A0A1G8ZUT1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:SDK18889.1};
GN ORFNames=SAMN05421869_114189 {ECO:0000313|EMBL:SDK18889.1};
OS Nonomuraea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=633440 {ECO:0000313|EMBL:SDK18889.1, ECO:0000313|Proteomes:UP000199202};
RN [1] {ECO:0000313|EMBL:SDK18889.1, ECO:0000313|Proteomes:UP000199202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDK18889.1,
RC ECO:0000313|Proteomes:UP000199202};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNDJ01000014; SDK18889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8ZUT1; -.
DR STRING; 633440.SAMN05421869_114189; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000199202; 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:UP000199202};
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 607 AA; 64525 MW; A84986EF11E022E1 CRC64;
MAELDLHYLT ELAAQLRVDS VRAAAAAGSG HPTSSMSAAD LMAVLFAGHL RYDFDRPDRP
ANDQLIFSKG HASPLLYSLY KACGVIDDEE LLSFRRRGSR LEGHPTPRLP WVDVATGSLG
QGLPVGVGVA MAGRLARLPY RVWVLCGDSE LAEGSIWEAA EHAGCEGLDR LTAIVDVNRL
GQRGPTRHGW DTGAYARRFG AFGWHTIEID GHDPVQIDQA LTDAANPRGR PTVILARTRK
GEGAPEVEDR EGAHGKALRD PDKAIDELGG TRDLRITVHE PPADVPRRFE DGPMSLPAYQ
VGEKVATRTA YGAALAALGQ ARGDVVALDG EVADSTKTEE FGKALPERFF EMYIAEQQLV
AAAVGLRIRG WTPYAATFAA FLTRAHDFIR MAAVSRASIR LVGSHAGVSI GEDGPSQMGL
EDLAMLRTVH GSTVLYPCDG NQAAALTVEM ADVDGVAYLR TTRGDTPVIY PPGERFPVGG
SRVLRHSPDD RATILAAGVT VHEALAAADD LAADGIPVGV IDLYSVKPVD SAALIEAATT
TGNLVTVEDH RLEGGLGDAV MDAVSELGPR VVKLAVTDLP GSATPREQLA DAGIDRHAIA
EAVKRSL
//
