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Database: UniProt
Entry: A0A0B0KJ59_9GAMM
LinkDB: A0A0B0KJ59_9GAMM
Original site: A0A0B0KJ59_9GAMM 
ID   A0A0B0KJ59_9GAMM        Unreviewed;       334 AA.
AC   A0A0B0KJ59;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:KHF75781.1};
GN   ORFNames=PJ15_1983 {ECO:0000313|EMBL:KHF75781.1};
OS   Acinetobacter sp. neg1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1561068 {ECO:0000313|EMBL:KHF75781.1, ECO:0000313|Proteomes:UP000030886};
RN   [1] {ECO:0000313|EMBL:KHF75781.1, ECO:0000313|Proteomes:UP000030886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=neg1 {ECO:0000313|Proteomes:UP000030886};
RA   Chiara M., Horner D.S., Pesole G., Mule' G., Logrieco A., Fanelli F.;
RT   "Genome Sequencing of an Acinetobacter spp capable to degrade OTA.";
RL   Submitted (NOV-2014) 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:KHF75781.1}.
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DR   EMBL; JSZD01000020; KHF75781.1; -; Genomic_DNA.
DR   RefSeq; WP_047432282.1; NZ_JSZD01000020.1.
DR   AlphaFoldDB; A0A0B0KJ59; -.
DR   PATRIC; fig|1561068.3.peg.2983; -.
DR   Proteomes; UP000030886; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          27..191
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  36182 MW;  CC9B5DE39E20EB23 CRC64;
     MSQLANPPKK KLTTSAMIAS IAAEGQPTKP APFGHALNAL AKERDDIVGL SADLSKYTDL
     HIFAKENPDK FFQMGMAEQL LMSAAAGLAR EGFVPFATTY AVFASRRAYD FICMAIAEDN
     LNVKIVAALP GLTTGYGPSH QATDDIAIFR AMPNLMIIDP CDALEIEQAI SQIAAHNGPV
     YMRLLRGQVP LVLDKYNYQF KLGKAQVIKP GKDLLIISTG LLTMRALEAA EELEKEGIEV
     SVLHVPTIKP LDEQTIWDEV SKGSRPVLTA ENHSVIGGLG EAVGSLLLRN GQHPRFDMIG
     LPDAFLDAGA LPTLHDRYGI STEAVKEKIK AHLK
//
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