GenomeNet

Database: UniProt
Entry: A0A136MT11_9BACT
LinkDB: A0A136MT11_9BACT
Original site: A0A136MT11_9BACT 
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
//
DBGET integrated database retrieval system