ID A0A1F6M3W5_9BACT Unreviewed; 644 AA.
AC A0A1F6M3W5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=A3B90_01710 {ECO:0000313|EMBL:OGH66280.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_41_13.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798676 {ECO:0000313|EMBL:OGH66280.1, ECO:0000313|Proteomes:UP000178742};
RN [1] {ECO:0000313|EMBL:OGH66280.1, ECO:0000313|Proteomes:UP000178742}
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=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 -!- 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:OGH66280.1}.
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DR EMBL; MFPX01000021; OGH66280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6M3W5; -.
DR STRING; 1798676.A3B90_01710; -.
DR Proteomes; UP000178742; Unassembled WGS sequence.
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; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
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 318..482
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 644 AA; 71408 MW; F1EA4D838F044515 CRC64;
MPVSTKQLEL LEAFAMSCRR SIIEMTSNAK SGHPGGSLGS IDYLTLLYTS IICKTNEPIV
ISNGHISPAL YAVLAELGAI NKKDLIKNFR HSGSIFEGHV ARSVPGVWYG TGPLGIGASV
ASGFALAQKL QKQNKKVFVT LGDGESEEGQ IYEMMNFATK YKLNNLIAFV DLNHVQLSDS
VQNVMPHDLH KIFTACGWEV ITVDGHSFQK LSQALGQAYK SKNKPVVILG ETIMGRGVSF
MENTGRLQQS TWHGTAPTKE QTQKALLELT LTKKQEEILA NFKKQNTWKA NKTQDIKTLT
KLKIKTGIAK TYSATDSLDC RTAYGKALLD LGKLNSNIVA LTADLAESVK TNFFKEKFPA
RHIECGIAEQ HMLSCAGGLS LSGFIPFAST YGVFMTSRAK DQARVNDINK TNVKMVATHC
GLSVGEDGPT HQAIDDIGSM LGFFNTMIIE PSDPNQTDHI IRYVANRYGN FYVRMGRHKV
PVLTKEDGSP FFDAKYKYQY GRSDILRPGK DLTLCASGSM VCEAYKAYEN LQKSHPKISI
ELVIINSPKI FDATIIESVK KTKKVLTLED HNTHSGFGSE LARHIITKNI SIQKFEMMGA
DEYQMSSTAQ ELYKSAKISS EFIEQKILQM LQDKKKSTRT FFFF
//
