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Database: UniProt
Entry: A0A166SE29_9ACTN
LinkDB: A0A166SE29_9ACTN
Original site: A0A166SE29_9ACTN 
ID   A0A166SE29_9ACTN        Unreviewed;       627 AA.
AC   A0A166SE29;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:OAA28040.1};
DE            EC=2.2.1.1 {ECO:0000313|EMBL:OAA28040.1};
GN   ORFNames=UG55_100612 {ECO:0000313|EMBL:OAA28040.1};
OS   Frankia sp. EI5c.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA28040.1, ECO:0000313|Proteomes:UP000077018};
RN   [1] {ECO:0000313|EMBL:OAA28040.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA28040.1,
RC   ECO:0000313|Proteomes:UP000077018};
RX   PubMed=27389275;
RA   D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA   Tisa L.S.;
RT   "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT   Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT   Nodules of Elaeagnus angustifolia.";
RL   Genome Announc. 4:e00660-16(2016).
RN   [2] {ECO:0000313|EMBL:OAA28040.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA28040.1,
RC   ECO:0000313|Proteomes:UP000077018};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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}.
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:OAA28040.1}.
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DR   EMBL; LRTK01000006; OAA28040.1; -; Genomic_DNA.
DR   STRING; 683316.UG55_100612; -.
DR   PATRIC; fig|683316.3.peg.778; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000077018; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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:UP000077018};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAA28040.1}.
FT   DOMAIN          318..480
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   627 AA;  65955 MW;  AF161B4F581F11C3 CRC64;
     MATPVSDVVG VADLXTVREL AQQLRVDSVR SSTSAGSGHP TSSMSAADVM AVLLTRHLRY
     DWDKPDDPAN DHLIFSKGHA SPLIYSMFKA VGVISDDELM TGYRRFGHRL QGHPTPILPW
     VDVATGSLGQ GLPDAVGVAL AGKFLDKVPY RVWVVCGDSE MAEGSMWEAL DKASFYGLSN
     LIAIVDVNRL GQRGPTELGW DLAAYARRVE AFGARAVTID GHDLGAIDAA LADAEDASRP
     TVILARTRKG DGFSEVADAE GWHGKPFSED MAARAIVELG GERNLRVRGP VPPADFPRPA
     PPVHPAVTLP TYELGAKVAT RRAYGQALAA VGVRTDVVAL DAEVSNSTYS EDFTKAHPDR
     FFEIFIAEQQ LVAAAVGLAV RGYIPFASTF AAFLSRAYDF IRMAAISQAD IRLSGSHAGV
     EIGPDGPSQM ALEDLAMMRA VGGSTVLYPS DATSAAKLVE AMTEISGVSY LRTTRGAYPV
     LYGPDETFAP GGSKVLRSSE ADTVTLVGAG VTLHHCLAAA DVLASEGVSA RVIDLYSVKP
     VDAATLAEAA RATGGRLVVV EDHYPEGGLG AAVLEGLAGV LRDGSVSLRL AHLAVTELPG
     SGTPDELLDF AGISAPHIAE AARGLLR
//
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