ID   A0A0C1V1R5_9ACTN        Unreviewed;       650 AA.
AC   A0A0C1V1R5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=MB55_00380 {ECO:0000313|EMBL:KIE53795.1};
OS   marine actinobacterium MedAcidi-G3.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE53795.1, ECO:0000313|Proteomes:UP000031370};
RN   [1] {ECO:0000313|EMBL:KIE53795.1, ECO:0000313|Proteomes:UP000031370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KIE53795.1}.
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DR   EMBL; JUEP01000001; KIE53795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1V1R5; -.
DR   STRING; 1550402.MB55_00380; -.
DR   Proteomes; UP000031370; Unassembled WGS sequence.
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; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          348..517
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   650 AA;  68766 MW;  99863CBB4893FD6A CRC64;
     MTSDLEIRQI NTIRALALDA VKKANSGHTG TAMALAPLAH VLFTKVMKYD SSVPSWPDRD
     RFILSAGHAS MLLYSMLYLT GFGLELDDIK DFRQMGSRTP GHPEVGATPG VEVTTGPLGQ
     GIANAVGMGL AERHLKERLG SDVVDHKIWT ICGDGDLMEG VSHEAASLAG HQKLGNLVVI
     YDDNRITIDG TTDLAMSDNA EKRFEAYGWN VRNLGEASED TELLEEALLG AANETDKPTL
     LILQSHIGFP APNAVDTPAA HGAITDDIEI LGAKSAMGMD PDATFNVDED VLAAYRAAGT
     RGATAREKWS DQVASSDLSR TWIDTLLTGS PIANWSDELP IYEAGTSLAT RNANSQVLDA
     IADAVPSLVS GSADLTGNTG TNIASEPMTA DCPDGRKLYY GVREHGMGSI ANGMALHGGI
     IPVVGTFLVF ADYMRPSVRM AALSSAKVIF VWSHDSIGVG EDGPTHQPVE QVASLRAIPD
     LTVIRPADGN EVSQAWEVAL NRTGPTALIL TRQNVPVLEG TVKANQVERG AYILIDPPDP
     VVILAGTGSE VQLCVEAAGA LAEDGVASRV VSMPSWELFH AQGEEYQRTV LPPGVPVVGV
     EAGVSLGWDR WADTTVTIDE FGASAPGDLV MEKFGITASN VEAAARSLLS
//