ID E7N114_9FIRM Unreviewed; 585 AA.
AC E7N114;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=HMPREF9555_00665 {ECO:0000313|EMBL:EFW30123.1};
OS Selenomonas artemidis F0399.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW30123.1, ECO:0000313|Proteomes:UP000004633};
RN [1] {ECO:0000313|EMBL:EFW30123.1, ECO:0000313|Proteomes:UP000004633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0399 {ECO:0000313|EMBL:EFW30123.1,
RC ECO:0000313|Proteomes:UP000004633};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFW30123.1}.
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DR EMBL; AECV01000008; EFW30123.1; -; Genomic_DNA.
DR RefSeq; WP_009349343.1; NZ_GL638132.1.
DR AlphaFoldDB; E7N114; -.
DR STRING; 749551.HMPREF9555_00665; -.
DR HOGENOM; CLU_009227_1_4_9; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000004633; 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; 63371 MW; D1C4641D21B88A8C CRC64;
MYLEKITSPA DIKGYDAAER KALAQEMRDA MLKRASIHGG HFGPDFGAVE AIIALHTVFD
SPKDKIVYDV SHQSYPHKML TGRVEAYIVE SQYDEVSGYT NPKESPHDFF NVGHTSTSIS
LATGLAKARD LAGRKENIIA FIGDGSMSGG EALEGLNTAG AMNSNLIVVF NDNDQSIAEN
HGGMYRAFKE LRETNGTSPN NLFRAMGLGY RYVADGNDAE ALIAAFSEVK DTEKPVVVHI
ATQKGKGYKF AEENREAWHY CGPFDIATGK AKHTGSDPYA KASVEFVLKT AKENPNFVYL
TAGTMGGIGL SPSKRAELGS QYVDVGIAEE QAVAMASGLA KGGARPIFGT YSTFFQRVYD
QVAQDVAVNN NPAVFLLVGA SMFYMNDVTH LGFFDIAIFA NIPNLVFLAP ASLAEYKAVL
AWSVAQTAHP VMIRMPVGGY EESPYAVRTD YSDLNKYEVV TEGADVAIIG AGNFASLASE
SAAELAKEGI RATVVNPIFL SGLDTALLDA LKEKHRLILT LEDGIIEGGF GQKIASYYGT
DEGLRVRNYG LSKEFHDRYD AAELAREHHL TAEQIAADTL ILLKK
//
