ID A0A1F6JWA7_9BACT Unreviewed; 334 AA.
AC A0A1F6JWA7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:OGH39124.1};
GN ORFNames=A3B44_01730 {ECO:0000313|EMBL:OGH39124.1};
OS Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_38_21.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798620 {ECO:0000313|EMBL:OGH39124.1, ECO:0000313|Proteomes:UP000178827};
RN [1] {ECO:0000313|EMBL:OGH39124.1, ECO:0000313|Proteomes:UP000178827}
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 -!- 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:OGH39124.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFOT01000007; OGH39124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6JWA7; -.
DR STRING; 1798620.A3B44_01730; -.
DR Proteomes; UP000178827; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
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 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 SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
FT DOMAIN 20..185
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 334 AA; 35957 MW; 5BA7EC73BA9D231C CRC64;
MLNPNLKLNP KIFDNNVEQK ATRTGYGEGL VELGEKNPNV VVLTADLSES TQTEAFEKKF
PERFFECGVA EQNMAAIAAG LGISGKIPFI SSYATFSPGK NWETIRTTIV YNQSNVKIAG
HHSGIVTGPD GATHQATEDI ASVRAWPGIT IFVACDAIEA KKATIKAAEI DGPVYLRFTR
DKTPVITTSE TPFDVGKIQT FWESDPSTGS GYQAVIFATG YILYNALLAA KELDTEGIEV
LVANVATIKP LDEKTVVELA EKTGAVVTAE DHQVMGGLGG AIAEVLAKNK PTPMEFIGLQ
NTFAESGTPK ELMEKYKMDA PAIVEAVRKV IARK
//
