(data stored in SCRATCH zone)

SWISSPROT: Q13R23_PARXL

ID   Q13R23_PARXL            Unreviewed;       192 AA.
AC   Q13R23;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000256|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000256|HAMAP-Rule:MF_01984};
GN   ORFNames=Bxe_B2525 {ECO:0000313|EMBL:ABE33466.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33466.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33466.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33466.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of
CC       the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-
CC       polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase
CC       is metal-independent and links a dimethylallyl moiety from
CC       dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms
CC       of FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl phosphate + FMNH(2) = prenylated
CC       FMNH(2) + phosphate. {ECO:0000256|HAMAP-Rule:MF_01984}.
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01984}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01984}.
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DR   EMBL; CP000271; ABE33466.1; -; Genomic_DNA.
DR   RefSeq; WP_011490834.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13R23; -.
DR   STRING; 266265.Bxe_B2525; -.
DR   EnsemblBacteria; ABE33466; ABE33466; Bxe_B2525.
DR   GeneID; 4006979; -.
DR   KEGG; bxb:DR64_4852; -.
DR   KEGG; bxe:Bxe_B2525; -.
DR   PATRIC; fig|266265.5.peg.5180; -.
DR   eggNOG; ENOG4108UMA; Bacteria.
DR   eggNOG; COG0163; LUCA.
DR   HOGENOM; HOG000225437; -.
DR   KO; K03186; -.
DR   OMA; TMAHETD; -.
DR   OrthoDB; POG091H05SH; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051188; P:cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX_Pad1.
DR   PANTHER; PTHR43374; PTHR43374; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13R23.
DR   SWISS-2DPAGE; Q13R23.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01984};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01984};
KW   Lyase {ECO:0000313|EMBL:ABE33466.1};
KW   Prenyltransferase {ECO:0000256|HAMAP-Rule:MF_01984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   DOMAIN       10    171       Flavoprotein. {ECO:0000259|Pfam:PF02441}.
FT   NP_BIND      17     19       FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   NP_BIND      94     97       FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   BINDING      43     43       FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   BINDING     129    129       FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   BINDING     159    159       DMAP. {ECO:0000256|HAMAP-Rule:MF_01984}.
FT   BINDING     175    175       DMAP. {ECO:0000256|HAMAP-Rule:MF_01984}.
SQ   SEQUENCE   192 AA;  20757 MW;  0E51A9E4D316833C CRC64;
     MHFSAVPPRR LVVGISGASG VVYGVRLLQL LRQLDIESHL VMSRSAQVTL AHESPYSVAE
     VRALATVTYP NTDIGAAISS GSFPVMGMIV APCSIRTLSE ISTGVTSGLL SRAADVTLKE
     RRRLVLMVRE TPLHLGHLRS MTNVTEAGAI VYPPVPAFYA NPESLDDMVD HTLGRVLDLF
     GIETPVVHRW GM
//

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