ID A0A1F6N562_9BACT Unreviewed; 627 AA.
AC A0A1F6N562;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
GN ORFNames=A2983_00420 {ECO:0000313|EMBL:OGH78793.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPLOWO2_01_FULL_40_15.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798686 {ECO:0000313|EMBL:OGH78793.1, ECO:0000313|Proteomes:UP000177040};
RN [1] {ECO:0000313|EMBL:OGH78793.1, ECO:0000313|Proteomes:UP000177040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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 -!- 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:OGH78793.1}.
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DR EMBL; MFQH01000002; OGH78793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6N562; -.
DR Proteomes; UP000177040; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 312..476
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 488..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 68254 MW; F7D7AB54478EFD42 CRC64;
MKNTISQLAK LIRHHILTMT TTAGSGHPSS SLSATDLMTT LMFGGFFQYD IKNPEHPNND
RLIFSKGHAS PLFYALWAIA GGIPTDELNT LRKFGSRLEG HPTMKFPFTE AATGSLGQGL
SIGVGMALNA KYLDKLPYKT YVLLGDSELA EGSNWEAMMS AAHYKLDNLI AIVDVNRLGQ
RGQTMFGYDI KNYKKKIEAF GWKTIVIDGH NPKQIDKAFA QAAKVKGQPV AIIAKTTKGK
GVKCMENKEG WHGKTLNATE LQTALKDLGE VDLNLQGEIK KTKNLPSSFG LQRGKVKPFA
EIDSAQMYAE PLATRAAYGH ALVEMFPHFP NMVVLDAEVS NSTFAEQFKK QYPKHFFEMF
IAEQNMVGVA IGLARRGKIP FVSTFAAFFT RAADQIRMAR HSNANIKLIG SHCGVSIGED
GASQMGLEDI ALFRAIPDSV VLYPADHVSE EKLSICAAEH NGMVYLRTTR AAVAPIYQPN
QTFKIGGSHT LRSGSTHSAS SGQAGSPQTK DDVTIIAAGI TVYEALKAYE ELKKQNIFAR
VIDLYSIKPL DFETLKKAAA ETKCIITVED HYPEGGIGEA VTAALSTTGI KIISLAVKKL
PMSGKPNELL AYEEINAAAI IATIKSI
//
