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Database: UniProt
Entry: A0A0R2QQP0_9ACTN
LinkDB: A0A0R2QQP0_9ACTN
Original site: A0A0R2QQP0_9ACTN 
ID   A0A0R2QQP0_9ACTN        Unreviewed;       648 AA.
AC   A0A0R2QQP0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-APR-2018, entry version 15.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315};
GN   ORFNames=ABR78_07005 {ECO:0000313|EMBL:KRO52632.1};
OS   Acidimicrobiia bacterium BACL6 MAG-120910-bin40.
OC   Bacteria; Actinobacteria; Acidimicrobiia.
OX   NCBI_TaxID=1655586 {ECO:0000313|EMBL:KRO52632.1};
RN   [1] {ECO:0000313|EMBL:KRO52632.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL6 MAG-120910-bin40 {ECO:0000313|EMBL:KRO52632.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C.,
RA   Pinhassi J., Andersson A.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC       atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC       1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767580}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767589}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC       5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS00767582}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00315,
CC       ECO:0000256|SAAS:SAAS00767578}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS00767545}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRO52632.1}.
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DR   EMBL; LIBI01000075; KRO52632.1; -; Genomic_DNA.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   HAMAP; MF_00315; DXP_synth; 1.
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; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767552};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767590};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767585};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767540};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00635456};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00635485}.
FT   DOMAIN      330    495       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
FT   REGION      113    115       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      147    148       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       146    146       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       175    175       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      72     72       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     175    175       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     301    301       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     381    381       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   648 AA;  69987 MW;  00A533C67FF32D5A CRC64;
     MVLEVIRQPS DLRGLTTTEL EQLAAEIRDF IVAAVSETGG HLGSNLGAVE LTLALHRVFD
     SPRDAILWDT GHQAYIHKIV TGRRGGFSQL RQAGGISGYP SREESVHDFI ENSHASTVLS
     YAYGLAVARD AGQTPDRRHI VAVIGDGSMT GGMAYEALNN LGHSSKRVII VLNDNGRSYA
     PTISNLSQGA PGERVTRKLS KTLIGIRINP VYVRRQRKIE KFLKNIPLIG TQAERGMEAF
     KAGVREFLQP PAFFEALGVR YIGPIDGHDI EAMEHAFSAA EQRVEEGPVV IHVFTEKGRG
     YSPAEDDDEK HLHDAPIFDP INGPPKSVPT GYTEAFADTI IKLAEQDARI VAITAAMPGP
     TGLIQFQEHF PDRFFDVGIA EQHAVTAAAG MAMGGMRPVV ALYSTFLNRA WDQVVYDVAL
     HRLPVIFCID RAGITGDDGP SHHGVYDMAL LSKVPGMRVL APSSTQDLQQ MLSDAISLAD
     TGPVAIRYPK GLARNVDEND IGSGLQARKL INGTTQRVCI LAIGKMVGAA LEAAETLKSS
     NIDVTVWDVR SCAPLDPTMI SDAMQHDLVI TAEDGIRDGG IGMTIENTIN DTSNNMSKSS
     TAHKRPVVHV MGVPTKFVAT AKPKVILHQM GLDSEGIVAQ VLRALSND
//
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