ID R6TQU6_9FIRM Unreviewed; 584 AA.
AC R6TQU6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
GN ORFNames=BN626_00236 {ECO:0000313|EMBL:CDC70286.1};
OS Agathobacter rectalis CAG:36.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=1263079 {ECO:0000313|EMBL:CDC70286.1, ECO:0000313|Proteomes:UP000018162};
RN [1] {ECO:0000313|EMBL:CDC70286.1, ECO:0000313|Proteomes:UP000018162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:36 {ECO:0000313|Proteomes:UP000018162};
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 -!- 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 -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081}.
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:CDC70286.1}.
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DR EMBL; CBFV010000016; CDC70286.1; -; Genomic_DNA.
DR AlphaFoldDB; R6TQU6; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000018162; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02007; TPP_DXS; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
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; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF1; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF13292; DXP_synthase_N; 2.
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 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018162};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 278..444
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 584 AA; 64220 MW; 5D925FE6682017A9 CRC64;
MYLEKINGPE DVKKIKIDEL PVLAQEIRDA LLVRASKHGG HFGPNFGMVE ATIALHYVFE
SPKDKIVYDV SHQSYPHKML TGRKEAYLSE QHYDDVSGYT NPNESEHDFF TVGHTSTSVS
LAAGLAKARD LKGENGNVIA VIGDGSLSGG EALEGLDFAA ELQSNFIIIV NDNDMSIAEN
HGGLYQNLAL LRKTDGQTEC NLFKAMGLDY VYVDRGNDVA ALIKAFKEVK DSTKPVVVHI
NTLKGKGYAP AEKCKEQWHY SGPFDIETGK PLFDNVEEDY SSVTCEYLLE KMKNDSSVVA
ITSGTPTVMG FTEDKRKEAG SQFVDVGIAE ETAVALASGV AVNGGKPFYG VYSSFVQRTF
DQVSQDVCIN NSPITMVIYQ GSVYGMNDVT HLGFQDIPML SNIPNLVYLA PATKEEYLAM
LDWSMEQTSY PVAIKLPGGP MISDGSRVTK DFGRLNRYEV VQTGEKIAII GLGTFFELAK
EAAKLLKEEA KINATVINPY YITGLDEALL TKLKQNHDTV ITLEDGILDG GFGEKIARFY
GASNMKVMNY GLKKEFLDRY DVDAVLKENH LTAEQIVEDV LSIS
//
