ID A0A1J5FGX6_9BACT Unreviewed; 615 AA.
AC A0A1J5FGX6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:OIP59609.1};
GN ORFNames=AUK19_01795 {ECO:0000313|EMBL:OIP59609.1};
OS Candidatus Moranbacteria bacterium CG2_30_45_14.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1805255 {ECO:0000313|EMBL:OIP59609.1, ECO:0000313|Proteomes:UP000183500};
RN [1] {ECO:0000313|EMBL:OIP59609.1, ECO:0000313|Proteomes:UP000183500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_45_14 {ECO:0000313|EMBL:OIP59609.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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 -!- 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:OIP59609.1}.
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DR EMBL; MNYT01000024; OIP59609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FGX6; -.
DR STRING; 1805255.AUK19_01795; -.
DR Proteomes; UP000183500; 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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 313..476
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 615 AA; 67074 MW; 4590D31661B80CBB CRC64;
MSDIIQLEKL AKLIRYWSLL MSTEAKSGHP TSSLSATDLM TVLFFGNYLR FDTEDIQNPN
NDRIIFSKGH ASPLFYALWT VAGEIPQADL SQYRTFGSSL EGHPMPTFRM TEVAAGSLGQ
GLSVGVGMAL SAKYLDKTEA RIYVLLGDSE MAEGSVWEAM NSATYYGLDN LVGIVDINRL
GQRGETMFGH DIDEYEKRAV AFGWQTIVID GHSLEEIVKA YETATKSIGK PVMILAKTIK
GKGVSFLEDK EGWHGKALSK EEFEQAKREL GEVDLSLRGR FASPGILSVP NNVISAGEGN
VHIDSSYRKG ELVATRQAYG TSLATLGASV PEIVALDAEV SNSTFSDIFK KRYPDRFFEM
FIAEQNMVGV AIGLARRGKI PFVSTFAAFF SRAFDQIRMA QYSEANVKFV GSHAGVSIGQ
DGASQMGLED IALFRSVLNS VVLYPADAVA TERLVEIATK HKGLVYIRTT RAATPVLYDS
TEQFPIGGSK TLRSSNSDVL TLVSAGITLF EALQAADGFI QKGIGIRVID LYSIKPLDRE
ALLLAAKETQ AIITIEDHYP AGGIGEAVSA ELSRVQTPVH NLSVMRTPHS GSPEGLLQYE
NISRMAIQEK IQSLL
//
