ID A9WT39_RENSM Unreviewed; 717 AA.
AC A9WT39;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN OrderedLocusNames=RSal33209_2246 {ECO:0000313|EMBL:ABY23977.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23977.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CP000910; ABY23977.1; -; Genomic_DNA.
DR RefSeq; WP_012245642.1; NC_010168.1.
DR AlphaFoldDB; A9WT39; -.
DR SMR; A9WT39; -.
DR STRING; 288705.RSal33209_2246; -.
DR KEGG; rsa:RSal33209_2246; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
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; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABY23977.1}.
FT DOMAIN 371..551
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 717 AA; 76306 MW; 0F441175CE489690 CRC64;
MPQEQQEFSW TTLDQRAVDT IKVLAADAVE KVGNGHPGTA MSLAPAAYLI FQRLLKHDPG
DPQWAGRDRF ILSPGHSSLT LYIQLFLSGY GLELSDLEAL RTWGALTPGH PEYKHTKGVE
ITTGPLGQGL ASSVGFAYSQ RRMRGLFDAD AAPGTSPFDH NIWVIASDGD LQEGVTSEAS
SLAGHQELGN LVVVYDQNHI SIEDDTDIAY SEDVLKRYEA YGWHVQRVDW TKTGDYVEDV
EGLYHALIEA KNETSKPSII ALRTIIGWPS PTKQNTGKIH GSALGAEEVA GLKKVLGFGP
EKTFDVDPEV LAHAREVAAR GAEAHADWDK ELTSWQAGNP DGAALLDRIE SGALPTDWAG
ALPTFEAGKD VSTRAASGKV INAIASELPE LWGGSCDLAE SNNTTIEGAP SFVPSDRQTG
AWSGNPYGRV LHFGIREHAA AAIVNGIHLG GPTRAFSGTF LIFSDYQRPA IRLGALMGVP
SIYVWTHDSI GLGEDGPTHQ PVEQLASLRA IPGLDVVRPG DANEVAQAWK GILENRNNPA
GIVLTRQNIP TYARAAGAAT ASEFASADGV LKGGYVLAES TSINAAGEAS VATPEAILIA
TGSEVQLAVQ ARETLQAEGI PTRVVSMPCV EWFHAQSPEY RASVLPAAVK TRVSVEAGVA
MPWREFLGDS GRSISLEHFG ASADYKRLYA ELGITVETVV AAAKDSQQAA ASAAVAS
//
