ID G5GNZ6_9FIRM Unreviewed; 585 AA.
AC G5GNZ6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=HMPREF9334_00800 {ECO:0000313|EMBL:EHG21383.1};
OS Selenomonas infelix ATCC 43532.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG21383.1, ECO:0000313|Proteomes:UP000004129};
RN [1] {ECO:0000313|EMBL:EHG21383.1, ECO:0000313|Proteomes:UP000004129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG21383.1,
RC ECO:0000313|Proteomes:UP000004129};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas infelix ATCC 43532.";
RL Submitted (AUG-2011) 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:EHG21383.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACZM01000007; EHG21383.1; -; Genomic_DNA.
DR RefSeq; WP_006692250.1; NZ_JH376798.1.
DR AlphaFoldDB; G5GNZ6; -.
DR STRING; 679201.HMPREF9334_00800; -.
DR PATRIC; fig|679201.3.peg.807; -.
DR eggNOG; COG1154; Bacteria.
DR HOGENOM; CLU_009227_1_4_9; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000004129; 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); 2.
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 Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 277..442
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 585 AA; 64221 MW; 5866D9E96720A9DE CRC64;
MYLETIKSPA DIKGYTAEQR RVLAQEMRDA LLKRASVHGG HFGPDFGIIE AIIALHTVFD
SPTDKIVYDV SHQCYPHKML TGRVEAYIDE DKYGEVSGYT NPEESPHDFF NVGHTSTSIS
LASGLAKARD LAGRRENVIA LIGDGSMSGG EALEGLNVVG EMGTNFIIVF NDNDRSIAEN
HGGMYREFRR LRETNGTAPN NLFRAMGLDY RYVADGNDCE ALIAAFSAVR DSEKPVVVHI
ATQKGKGYKF AEEDPETWHY CSVFDIETGA LKHPYTDPYQ EATKAFLKEQ AETNPNFVFL
AAGTMGGIVL SPADRAELGS HYVDVGIAEE HAVAMASGLA RGGARPIFGT YSTFFQRVYD
QMAQDVAINN SPAVFLSVGA SLYYMNDVTH LGFFDIPIFA NIPNLVFLAP ASLDEYKAVL
RWSIAQTSHP VMIRMPVGGY EENPYDVRTD YSDLNTYQVV QEGAEVAIIG VGNFAALASE
AAALLEKEGI QATVVNPIFL SGLDTALLKR LKEKHRLILT LEDGILDGGF GQKIAAYYGM
DTQISVRNYG LSKEFHDRYR ASELARAHHL TAEQIAADTL SAWKG
//
