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Database: UniProt
Entry: R7KFH9_9BURK
LinkDB: R7KFH9_9BURK
Original site: R7KFH9_9BURK 
ID   R7KFH9_9BURK            Unreviewed;       603 AA.
AC   R7KFH9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=BN692_00822 {ECO:0000313|EMBL:CDE75125.1};
OS   Sutterella sp. CAG:521.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=1262977 {ECO:0000313|EMBL:CDE75125.1, ECO:0000313|Proteomes:UP000018289};
RN   [1] {ECO:0000313|EMBL:CDE75125.1, ECO:0000313|Proteomes:UP000018289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:521 {ECO:0000313|Proteomes:UP000018289};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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:CDE75125.1}.
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DR   EMBL; CBJP010000018; CDE75125.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7KFH9; -.
DR   STRING; 1262977.BN692_00822; -.
DR   Proteomes; UP000018289; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018289}.
FT   DOMAIN          287..459
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   603 AA;  66522 MW;  D4715FA349F6BF70 CRC64;
     MLQYALLHLT GYDLTIDDLK AFRQWHSKTP GHPEVDVTPG VETTTGPLGQ GIGNAVGMAL
     AEKMLAAEFN RPGFNVIDNY TYCFLGDGCL MEGISHEVCS LAGTWKLNKL IVIYDDNGIS
     IDGKVINWFS DNTRERFESY GWNVIGPVDG HDIDEMDRAI ATAKQSQDKP TLIIARTVIG
     KGSPNRQGTS KVHGEALGEE ELKLTREALG WKWDPFVIPQ EIYDAMNARE KGEKLEAEYN
     EMWARYGQEY PQLCKELSRR LKGDLPEDFE AVMQQAIEKA AVAQETVATR KASQKALNAF
     ASHLPELLGG SADLTGSNLT NWTGVEAMRP DTYLGRHINY GVREFGMSAI QNGIALYHGF
     VPFSATFLTF SDYSRNAIRM AALMKQRSIF VFTHDSIGLG EDGPTHQSVE HIPSLRLIPN
     LNVWRPCDTV EALVAWQSAI ESRHTPSIII GSRQNIEFIA RDPQEVVRDA KEALKAGAYV
     MKESGKGADE VDCVLIATGS EVPLAVKARE ALEEKGIGTR VVSMPCTELF DKLSSEEKRA
     ILTDAPKVAI EASVTGLWYK YVKNGEVVGI DTFGESAPAG VLWEKFGFTV DRVVEAAMKA
     INH
//
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