ID A0A133Y7D9_9FIRM Unreviewed; 727 AA.
AC A0A133Y7D9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative 1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:KXB39124.1};
GN ORFNames=HMPREF1872_01150 {ECO:0000313|EMBL:KXB39124.1};
OS Amygdalobacter nucleatus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Amygdalobacter.
OX NCBI_TaxID=3029274 {ECO:0000313|EMBL:KXB39124.1, ECO:0000313|Proteomes:UP000070080};
RN [1] {ECO:0000313|Proteomes:UP000070080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00274 {ECO:0000313|Proteomes:UP000070080};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KXB39124.1}.
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DR EMBL; LSCV01000042; KXB39124.1; -; Genomic_DNA.
DR RefSeq; WP_066714664.1; NZ_KQ959596.1.
DR AlphaFoldDB; A0A133Y7D9; -.
DR STRING; 1497955.HMPREF1872_01150; -.
DR PATRIC; fig|1497955.3.peg.1121; -.
DR OrthoDB; 9803371at2; -.
DR Proteomes; UP000070080; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02007; TPP_DXS; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR049557; Transketolase_CS.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF13292; DXP_synthase_N; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070080};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 344..509
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 727 AA; 80926 MW; DE158E116A60139A CRC64;
MKPTTSDSEF RLHIEQNYPL IAKVNLDLAN LKKFTATDLS QLCQELRAFI TEQVALHGGH
LASNLGVIEL TVALLRTYDF TKDRLIWDVG HQCYAWKILT YRASGFAHLR EKDGLAGFPK
PTESEFDHFG TGHATTSISA ALGMAAAFKE KGLDHKVIAV IGDGALTGGM AWEALNNISE
LEPNLLIVLN DNTMSIDKNV GFVADELGKL RLNAGYLAFK LKLKTKLNNL GQFGQTLLRI
GRLSKAKLRS KLGKTREFFC ERYGCRYYGP LNGHDLLQVE ASLQGLKTFK RPALLHIVTE
KGHGYAPATN DPTSFHGVKR NDERLLAACY EEPLKTKVEA NNKLSYTDAF QQMIMEMAEK
EDFACITAAM ASGTGLKAFS EKYPTRFYDV GIAEQHAVCF AAGLVSQGVK TVCAIYDTFL
QRALDAVIHD VCLQNLPLIL AIDRAGLVGQ DGATHQGIYS LAFLVALPNL KIINSSDPYM
LQVFLQQALK RKLNYPLALR YPRANLELPA FLPKARLAEY QLDRTYANVY EFVQTIPQNL
ETTTTDWSQI ENSVELAQFL KAHAYKLNQK VFVKTEQAAA KPTCKFALTI LTSGRLVTNC
LQALFDLISQ HKLEQPICLI DCFDYSLSLA ELKQSNSLLR SRLQVSERVL ILEESSGLSP
LYAALYTDLA DFKHWQVMEV KNLGNDVIEQ GEIPELLANY RLDRASLVED IPAILAKGKA
VKEAKSK
//