(data stored in SCRATCH zone)

SWISSPROT: Q13IA4_PARXL

ID   Q13IA4_PARXL            Unreviewed;       513 AA.
AC   Q13IA4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   SubName: Full=Putative radical SAM domain/B12 binding domain protein {ECO:0000313|EMBL:ABE36185.1};
GN   ORFNames=Bxe_C0261 {ECO:0000313|EMBL:ABE36185.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36185.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36185.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36185.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., 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).
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DR   EMBL; CP000272; ABE36185.1; -; Genomic_DNA.
DR   RefSeq; WP_011493445.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0261; -.
DR   EnsemblBacteria; ABE36185; ABE36185; Bxe_C0261.
DR   GeneID; 4009633; -.
DR   KEGG; bxb:DR64_8170; -.
DR   KEGG; bxe:Bxe_C0261; -.
DR   PATRIC; fig|266265.5.peg.8043; -.
DR   eggNOG; ENOG4105EPH; Bacteria.
DR   eggNOG; COG1032; LUCA.
DR   HOGENOM; HOG000014070; -.
DR   KO; K22704; -.
DR   OMA; FPTYHWR; -.
DR   OrthoDB; 973846at2; -.
DR   BioCyc; BXEN266265:BXE_RS37995-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR027564; HpnR_B12_rSAM.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00565; hopanoid_C3-methyltransferase_; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR04367; HpnR_B12_rSAM; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   4: Predicted;
DR   PRODOM; Q13IA4.
DR   SWISS-2DPAGE; Q13IA4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        8    141       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
SQ   SEQUENCE   513 AA;  58192 MW;  479E505926AF935F CRC64;
     MKVLTVHPSG LMYTRVFLRL EPLGLETVAA VLREAGHEVR LIDLQVETHR DLHRLIRNWQ
     PDAVCFSGNY LANIPEIVDL AKSVKEKQPR CFVFVGGHSV SFTAADILRH AEGAVDCVLK
     GEGEASVVAL LEAASHGADL LQIPGAVTQH GEGPPPHFVE SLDPVRPARD LLRHRRKYFI
     GTLDPCASIE FARGCPWDCT FCSAWTFYGR SYRARSPEVV AGELASIREP GVFIVDDVAF
     VHADHGMEIG KAVQRRGIRK KYYLETRGDV LLRNREVFEF WRGLGLQYMF IGMEAIDAEG
     LKAFRKRINL DRNFEALAFA RSLGITVAIN LIADPDWDHD RFEAVRQWCL EIPEIVNISV
     NTPYPGTEIW LREQRRLTSL DYRLYDIQHA VLPTRLPLPE FYAELVRTQQ VLNRKHLGWT
     ALRGAAGHAC HLLLRGQTNF VRMLWRFNSV FNPQLQLNDH AREVHYTMSP PPGITEQRID
     VKALYVHGPI GRKGRRIDDA TENFVEQTRM GAG
//

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