(data stored in ACNUC7421 zone)

HOGENOM: MOOTA_1_PE1014

ID   MOOTA_1_PE1014                       STANDARD;      PRT;   385 AA.
AC   MOOTA_1_PE1014; Q2RJN4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase; Short=DXP
DE   reductoisomerase; EC=1.1.1 267;AltName: Full=1-deoxyxylulose-5-phosphate
DE   reductoisomerase;AltName: Full=2-C-methyl-D-erythritol 4-phosphate
DE   synthase; (MOOTA_1.PE1014).
GN   Name=dxr; OrderedLocusNames=Moth_1041;
OS   MOORELLA THERMOACETICA ATCC 39073.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOOTA_1.PE1014.
CC       Moorella thermoacetica ATCC 39073, complete genome.
CC       7874984..8874983 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:DXR_MOOTA
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
CC       of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
CC       4-phosphate (MEP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
CC       = 1-deoxy-D-xylulose 5-phosphate + NADPH.
CC   -!- COFACTOR: Divalent cation (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 1/6.
CC   -!- SIMILARITY: Belongs to the DXR family.
CC   -!- GENE_FAMILY: HOG000007220 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q2RJN4; -.
DR   EMBL; CP000232; ABC19355.1; -; Genomic_DNA.
DR   RefSeq; YP_429898.1; NC_007644.1.
DR   ProteinModelPortal; Q2RJN4; -.
DR   STRING; Q2RJN4; -.
DR   GeneID; 3831847; -.
DR   GenomeReviews; CP000232_GR; Moth_1041.
DR   KEGG; mta:Moth_1041; -.
DR   NMPDR; fig|264732.9.peg.1023; -.
DR   eggNOG; COG0743; -.
DR   OMA; IHSMVEY; -.
DR   PhylomeDB; Q2RJN4; -.
DR   ProtClustDB; PRK05447; -.
DR   BioCyc; MTHE264732:MOTH_1041-MON; -.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00183; DXP_reductoisom; 1; -.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
DR   HOGENOMDNA; MOOTA_1.PE1014; -.
KW   Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome.
SQ   SEQUENCE   385 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKEITVLGS TGSIGRQTLE VVAAHPGRFR VAALVAARND ELLAAQVRRF RPRLAVLLDE
     ERARVLAEMV SDPGIRILAG EEGLMAAACL EGVELVVAAM VGIRSLKAIL AALEAGKDIA
     LANKEVLVAA GQLVMDRARR LSRQIIPVDS EHSAIFQCLR QGGRVAEVII TASGGPLRQM
     PRAEMANVTP EQALNHPTWV MGPKITIDSA TLMNKGLEVI EAKHLFNLDF DQIKVLIHPQ
     SVVHALVRYS DGALFAQLGP ADMRLPIQYA LTWPERWDLD VQPLDLAALG HLEFALPDLE
     RFPCLELALQ AGRAGGTYPA VLSAADEVAV EYFLAGKITL TAISQVVGRV LDEHQPEPVP
     DLEGILAADA WARRRAGAVA EGLSF
//

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