ID A0A1F6V9P6_9BACT Unreviewed; 644 AA.
AC A0A1F6V9P6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=A2647_01880 {ECO:0000313|EMBL:OGI66341.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_40_24b.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801739 {ECO:0000313|EMBL:OGI66341.1, ECO:0000313|Proteomes:UP000177370};
RN [1] {ECO:0000313|EMBL:OGI66341.1, ECO:0000313|Proteomes:UP000177370}
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 -!- 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:OGI66341.1}.
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DR EMBL; MFTP01000001; OGI66341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6V9P6; -.
DR SMR; A0A1F6V9P6; -.
DR Proteomes; UP000177370; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF4; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF02779; Transket_pyr; 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.
PE 3: Inferred from homology;
FT DOMAIN 342..506
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 644 AA; 70145 MW; DBBCF2039EC8BED9 CRC64;
MKSIKIPFSL KDSELDVLAV YLRKRVFEIC LKAHNGHIGG SSGAVELMTA LYFGGFLRLN
LKDPSCPKRD RVLVRGHLGP IRYPILSLLG FIMPEELDAY RQFGSRLHGH EDHQEVPGVD
ITPSGSLGMI LSYGVGSAIA ANKRQDPFTT FVFLGDGEEQ EGNVSEAARH AAQLRLKHLV
VIIDCNGKQL SDPVIKADAS NLALIWKGYG WNVIKLPNGQ DVSAIRRVYT KALKSANDGS
VVIIANTLKG VGLKEALTHF SGYHTISTCK EGIVMDAIHK QESMINYPLL AKVLRKIGSV
VGQSSLGKSV ITSGSNQAQS PEVLFDIQPL AMTPNNPDLS QADYFRQLGS VWQSEGLPKG
YFLSADVTRR DHVKLLGLSR FAKYMNTGIR EQHTIAMAHG LSITDPRARI IINSLDAFTY
RAMDQINAMV QGGGRAVIIA DVAGLSNSKN GKTHQSSGQP GAIIMMPGIA FLEPWDVVDT
FNCLNWAIGH GIGVVFVRIH SSWIDVKVQS SVNRNIDHYC VFEPTASLQC SIVASGLTVS
SAIKAARTLD QEGVGVQVIN VINHKGIESI DFPPGKPVLT VYNGNPHVLQ SAVAMQAMRA
SHAPSRIEGI GFEFGTTGDI FELVKKFQLD EHSIVRKIRS ELLK
//
