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Database: UniProt
Entry: K1JKG4_9BURK
LinkDB: K1JKG4_9BURK
Original site: K1JKG4_9BURK 
ID   K1JKG4_9BURK            Unreviewed;       662 AA.
AC   K1JKG4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=HMPREF9465_01718 {ECO:0000313|EMBL:EKB30671.1};
OS   Sutterella wadsworthensis 2_1_59BFAA.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB30671.1, ECO:0000313|Proteomes:UP000005835};
RN   [1] {ECO:0000313|EMBL:EKB30671.1, ECO:0000313|Proteomes:UP000005835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB30671.1,
RC   ECO:0000313|Proteomes:UP000005835};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL   Submitted (MAY-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:EKB30671.1}.
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DR   EMBL; ADMG01000037; EKB30671.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1JKG4; -.
DR   STRING; 742823.HMPREF9465_01718; -.
DR   PATRIC; fig|742823.3.peg.1713; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_4; -.
DR   Proteomes; UP000005835; 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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005835};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          350..521
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   662 AA;  71773 MW;  5529D2EB1A3B5448 CRC64;
     MMANAIRALS MDAVQKAKSG HPGMPMGMAD IATALWSRHL RFNPTNPKWT GRDRFILSNG
     HGSMLQYALL HLTGYDLSID DLKAFRQLHS KTPGHPEVDV TPGVETTTGP LGQGIANGVG
     MALAEKMLAN EFNREGFPVF DNRTYVFLGD GCMMEGISHE VCSLAGVWKL NKLIAIYDDN
     GISIDGDVKG WFGDDTRGRF EAYGWNVIGP VDGHDIDAMD AAIAEAKLSE DKPTLIIART
     TIGKGSPNRQ GTAKVHGEAL GDEEIAATRA AIGWPYAPFE VPQEVYDAWD HRAEGARIEA
     EWQTMFDGYA AQYPELAAEL KRRLAGDLPE NWSDTVMDAL CAAEEAAETV ATRKASQKAL
     NALAPALPEL LGGSADLTGS NLTNWTGVKS LNSGDFLARH ISYGVREFGM SAIMNGIALY
     GGFIPYAATF LTFSDYSRNA LRMSSLMKQR VINVFTHDSI GLGEDGPTHQ SVEHVPSLRL
     IPGMHVWRPA DTVETIIAWA SAIERRNGPS CLVFTRQNVP FLDRDEVDAD AIARGAYVAA
     EAPAGAGEAE VVLLATGSEV GLAMKARAEL TARNVQVRVV SMPCANLFDE QDEEYRRAVL
     PEGVPVLAIE ASKSDLWYKY FSGKGAVIGV DTFGESAPAC VLWERFGFTV ENVVAKVEQL
     LK
//
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