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Database: UniProt
Entry: A0A133Y7D9_9FIRM
LinkDB: A0A133Y7D9_9FIRM
Original site: A0A133Y7D9_9FIRM 
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
//
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