ID A0A0Q4MRG6_9GAMM Unreviewed; 317 AA.
AC A0A0Q4MRG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KQN55485.1};
GN ORFNames=ASF13_08210 {ECO:0000313|EMBL:KQN55485.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN55485.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN55485.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN55485.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN55485.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN55485.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN55485.1}.
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DR EMBL; LMLK01000022; KQN55485.1; -; Genomic_DNA.
DR RefSeq; WP_056237479.1; NZ_LMLK01000022.1.
DR AlphaFoldDB; A0A0Q4MRG6; -.
DR STRING; 1736225.ASF13_08210; -.
DR Proteomes; UP000050856; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 5..170
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 317 AA; 33004 MW; 2CB255D1BDE12F53 CRC64;
MSEKKHLATV MVEALIDAVN DGVDVVPVVA DSTSTAKIGP FLKAFPGRTV NVGIAEQVLV
GTAAGLALGG KVAVTCNAAP FLISRANEQI KVDVCYNNTN VKLFGLNAGA SYGPLASTHH
STDDIAVMRG FGNIEIYAPS CPAECRQIID YALRHTGPVY IRLDGKDLPV LHDEQYQFTP
GKIDVLRTGS DVALVALGSA VHEAVDAAAQ LSELGIQATV VSVSSVRPCD TAELARVIGD
IPQVISVEEH NINGGVGSLV AEVIAENGLR ARLKRLGVTD GGYAIAGDRQ STRVGLGIDA
ASVRDTATAL VKGENRA
//
