ID A0A136MT11_9BACT Unreviewed; 279 AA.
AC A0A136MT11;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Transketolase 1 {ECO:0000313|EMBL:KXK37039.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:KXK37039.1};
GN Name=tktA {ECO:0000313|EMBL:KXK37039.1};
GN ORFNames=UZ16_OP3001001241 {ECO:0000313|EMBL:KXK37039.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK37039.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK37039.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK37039.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KXK37039.1}.
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; LMZT01000060; KXK37039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MT11; -.
DR STRING; 1617433.UZ16_OP3001001241; -.
DR PATRIC; fig|1617433.3.peg.1342; -.
DR Proteomes; UP000070296; Unassembled WGS sequence.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXK37039.1}.
FT DOMAIN 15..273
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 279 AA; 30790 MW; B27A5592AEF27265 CRC64;
MASCCQSTPD AAHLKEIARK TRIQVIQMLA EAGSGHPGGS LSACDVMTVL LNRFMRHDPK
NPRWEDRDRF VLSKGHCVPA WYSLLAQAGY FPEEQLMTLR KLGSPLQGHP DCNTMESMEA
CTGSLGQGLS IAVGMALAGK LDKKDYRVYC MIGDGETQEG QIWEAFMSAP KFKLDNLIVI
LDNNKGQIDG PVEEVMPLQP IVEKLRAFNW HVIDIDGHDL DKIIAAFDEA LKVKDKPIFI
RADTIKGKGV SFMEGGIDWH GRAPKPEEAE KAVKELSAA
//