ID   A0A0K1FDS4_9MICO        Unreviewed;       739 AA.
AC   A0A0K1FDS4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=ADJ73_13110 {ECO:0000313|EMBL:AKT52845.1};
OS   Arsenicicoccus sp. oral taxon 190.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Arsenicicoccus.
OX   NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52845.1, ECO:0000313|Proteomes:UP000065578};
RN   [1] {ECO:0000313|Proteomes:UP000065578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-2015) 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}.
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DR   EMBL; CP012070; AKT52845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K1FDS4; -.
DR   STRING; 1658671.ADJ73_13110; -.
DR   KEGG; ars:ADJ73_13110; -.
DR   PATRIC; fig|1658671.3.peg.2671; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000065578; Chromosome.
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}.
FT   DOMAIN          386..566
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          420..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  79545 MW;  69FD6CD7F01827A0 CRC64;
     MTPKANGRQV SDIVADTVGW DDVDVRAVDT VRCLAADAVQ KTGNGHPGTA MSLAPAAYLL
     YQNVMRHDPT DPHWMGRDRF VLSAGHSSLT QYIQLYYAGL LELDDIKALR TWGSKTPGHP
     EVHHTEGVDL TTGPLGSGVA TAVGMAMAQR RQRGMFDPDA APGESVFDHR VYCIAGDGCM
     MEGVASEASS LAGTQRLGNL TLIYDQNQIS IEDDTDVAFS EDVAKRYEAY GWDVRVVEWR
     TRHGVRDEDY VEDVDALFAA IEEGHKVLDR PTFIMLRTVI AWPAPTKQGT GKAHGAALGD
     DEIKAMKSLL GFDPEQTFEV SPEVEKRVRE VRDRGAKAHR EWEERYQAWR AGAPDKAALV
     DRLLAQELPE GFAEAFPTFE PDDKGLATRA ASGKVLGALA EIMPELWGGS ADLAESNNTT
     MTGQPSFVPE DRQTEEWRGG PYGRTIHFGV RENAMGMIVN GISLEGLTRA YGGTFLVFSD
     YMRPAVRLAA IQETDSIFVW THDSIGLGED GPTHQPIEHL AALRAMPNLD VVRPADANET
     AHAWKRILEG HGTPTGIALS RQALPTIAPA DTSADKVAKG AYVLVEGSKP TPDVIVMATG
     SEVSVAVAGA EQLEAAGIAT RVVSMPCLEW FARQDADYRE SVLPAAVKAR VSIEAGATMG
     WRDYVGDAGR IIGIDHFGAS ADAKTLFREF GFTPEAVVEA AKASIAGAAS ATPGDTAPGY
     ATSDPGFETS APAERQEGK
//