ID   A0A3A5LY18_9MICC        Unreviewed;       734 AA.
AC   A0A3A5LY18;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=D6T63_16500 {ECO:0000313|EMBL:RJT76515.1};
OS   Arthrobacter cheniae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1258888 {ECO:0000313|EMBL:RJT76515.1, ECO:0000313|Proteomes:UP000272560};
RN   [1] {ECO:0000313|EMBL:RJT76515.1, ECO:0000313|Proteomes:UP000272560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hz2 {ECO:0000313|EMBL:RJT76515.1,
RC   ECO:0000313|Proteomes:UP000272560};
RA   Liu Q., Xin Y.-H.;
RT   "Novel species of Arthrobacter.";
RL   Submitted (SEP-2018) 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:RJT76515.1}.
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DR   EMBL; QZVT01000011; RJT76515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5LY18; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000272560; 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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RJT76515.1}.
FT   DOMAIN          378..558
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          708..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  78515 MW;  A33C1B540E5EEB23 CRC64;
     MNPTANATLT EDPTLTWTEL DQRAVDTVRV LAADAVEKVG NGHPGTAMSL APAAYVLFQK
     LLRHDPSDPE WTGRDRFVLS PGHTSLTLYI QLFLSGYGLE LDDLKALRTW GSLTPGHPEY
     RHTKGVEITT GPLGQGLATA VGFAYGQRRQ RGMFDPEAAA GTSPFDHTIW VIASDGDLQE
     GVTSEASSLA GHQELGNLVV IYDENHISIE DDTDVAFTED VLKRYEAYGW HTQRVDWTKT
     GKYVEDVAEL YSALVAAKAE TSKPSIVSLR TIIGYPAPKK QNTGKIHGSA LGKDEVAALK
     EVLGFDPEKH FEVDPEVLEH ARGVVQRGAQ AHAAWQEGFD AWQASHAEEA AVLERIQART
     LPAGWDASLP SFEAGKDLST RAASGKVLTA IGPVLPELWG GSADLAESNN TTIEGAASFI
     PESRQTASWK GNPYGRVLHF GIREHAAAAI VNGIVMHSST RAFSGTFLIF SDYQKPAVRL
     GALMGVPAIY VWSHDSIGLG EDGPTHQPVE QLASLRTIPG LDVVRPGDAN EVAVAWRTIL
     ENTQNPAGIV LTRQNIPVYE RGDGPATGTT FGSAEGVARG GYVLAEASTD TPDVILIGTG
     SEVQLAVEAR ETLEAQGISA RVVSMPCLEW FNAQDAAYRN SVLPRTVRAR VSVEAGVSQS
     WQGIVGDAGR SVSLEHFGAS ADYKTLYREF GITADAVVQA AKDSIEATTT DPLAPNGTPA
     MASGHQATET GDQL
//