ID A0A1Q5E836_9ACTN Unreviewed; 622 AA.
AC A0A1Q5E836;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:OKJ04294.1};
GN ORFNames=AMK18_03695 {ECO:0000313|EMBL:OKJ04294.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ04294.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKJ04294.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKJ04294.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ04294.1}.
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DR EMBL; LISW01000001; OKJ04294.1; -; Genomic_DNA.
DR RefSeq; WP_073861616.1; NZ_LISW01000001.1.
DR AlphaFoldDB; A0A1Q5E836; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000186839; 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:UP000186839};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 318..480
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 622 AA; 65797 MW; 718F0E51FABAE19D CRC64;
MTSEQTSTLG PDSDLTEVFE LAQQLRVDSV RASTSAGSGH PTSSLSAADL MAVLMTRHLR
YDWNAPENPA GDHLVFSKGH ASPLLYAMFK AAGAISDEEL MTTYRRFGHR LQGHPTPELP
WVDVATGSLG QGIAYGVGIA LAGRDLENQP YRVWVLCGDS EMAEGSVWEA LDKAGQHRLG
NFTAIIDVNR LGQSGPTELQ WDTDTYARRV EAFGCRALVV DGHDLTEVDR ALKTAADGTA
PTVIVAKTVK GRGVSEVADK EGWHGKPLPE DLAERAIEEL GGVRDLRVEG PRPPKAAPAP
ARSDAAVELP RFEKGDEVAT RVAFGKALVA LGVRPDVVAL DAEVGNSTHS EDFKKAYPDR
FFQTYIAEQQ MVAEAVGMAV RGFRPYATTF AAFLTRAHDF IRMAAVSDIT MALCGTHSGV
EIGADGPSQM GVEDLAMMRA VRGSTVLYPS DATSAAALTV AMADIDGISY LRTTRGAYPV
LYGSDETFPV GGSKTLRHGD DDQVTLVGAG VTLHECLAAA DLLAEQGVRA RVIDLYSVKP
LDSGALALAA RETGALVVVE DHHPEGGIGE AVLSSLAESG SHPGFVHLAG SNLPGSGTTP
ELLDAAGISR THIADAARSL VK
//