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Database: UniProt
Entry: R7XZL9_9ACTN
LinkDB: R7XZL9_9ACTN
Original site: R7XZL9_9ACTN 
ID   R7XZL9_9ACTN            Unreviewed;       641 AA.
AC   R7XZL9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=CF8_1515 {ECO:0000313|EMBL:EON24475.1};
OS   Nocardioides sp. CF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=110319 {ECO:0000313|EMBL:EON24475.1, ECO:0000313|Proteomes:UP000015971};
RN   [1] {ECO:0000313|EMBL:EON24475.1, ECO:0000313|Proteomes:UP000015971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF8 {ECO:0000313|EMBL:EON24475.1,
RC   ECO:0000313|Proteomes:UP000015971};
RX   PubMed=23833136;
RA   Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT   "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT   of Its Metabolic Capabilities.";
RL   Genome Announc. 1:e00439-e00439(2013).
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:EON24475.1}.
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DR   EMBL; ASEP01000048; EON24475.1; -; Genomic_DNA.
DR   RefSeq; WP_010832477.1; NZ_CM001852.1.
DR   AlphaFoldDB; R7XZL9; -.
DR   STRING; 110319.CF8_1515; -.
DR   PATRIC; fig|110319.3.peg.2103; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_11; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000015971; 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; 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; 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:UP000015971};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          357..526
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   641 AA;  68065 MW;  20DF57AD4B823DCA CRC64;
     MTDVLQTEHT TVETDRLAVD TLRFLAADMV QAANSGHPGM PMGAAPMAWA LWSRHLRHDP
     ADPAWADRDR FVLSAGHGSA LLYGLLHIFG YDLPTEELRA FRQLGSRTPG HPEFGHTPGV
     ECTTGPLGQG LAMAVGMALA ERMSAARFPR VTDHRTYAIV GDGCLMEGVS HEAGSFAGHL
     GLGGLVVLWD DNSITIDGAV DRSCSDDQLA RFAAYGWHTE QVLDGTDVEA IHEAITRAEA
     DPRPSFIAVR TVIGQGAPGV EGTSKAHGSP LGEELLAETK RLAGWDHEAF TVPEPVRAAC
     AALAADGARA HAEWDKTFAA FADAEPEVAA QFTRALGRAL PADLEEVLGG AVGDAPRATR
     QSSQACLNAL RDALPELVGG SADLAGSTGT SFGDVITRDD FGRRAIGFGI REFGMATFMN
     GISLHGGFRV FGSTFLVFAD YLRPALRLSA LMKQPVVYVF THDSIAVGED GPTHQPITHI
     ESLRIIPGLQ VLRPADDAET ARAWQLALER TDGPTALVLS RQSLPQLDRA TFESDSPVTL
     EIVATGSEVA LAAAVAEVFR GEGYGVRVVS PFDRSRYTPD PSATRVSIEA GSTSAWSGIA
     DVAIGIDDFG ASGPGEDVLA FHGFTVDNVV AKIREHLATR R
//
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