(data stored in SCRATCH zone)

SWISSPROT: Q13J10_PARXL

ID   Q13J10_PARXL            Unreviewed;       297 AA.
AC   Q13J10;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 59.
DE   SubName: Full=Putative membrane protein {ECO:0000313|EMBL:ABE35929.1};
GN   ORFNames=Bxe_C0001 {ECO:0000313|EMBL:ABE35929.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35929.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35929.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35929.1,
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; ABE35929.1; -; Genomic_DNA.
DR   RefSeq; WP_011493189.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0001; -.
DR   EnsemblBacteria; ABE35929; ABE35929; Bxe_C0001.
DR   GeneID; 4009808; -.
DR   KEGG; bxe:Bxe_C0001; -.
DR   PATRIC; fig|266265.5.peg.7779; -.
DR   eggNOG; ENOG4105ECS; Bacteria.
DR   eggNOG; COG3000; LUCA.
DR   HOGENOM; HOG000262203; -.
DR   OMA; WRHRISH; -.
DR   OrthoDB; 2048011at2; -.
DR   BioCyc; BXEN266265:BXE_RS36765-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   4: Predicted;
DR   PRODOM; Q13J10.
DR   SWISS-2DPAGE; Q13J10.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     39       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     60     80       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    100    122       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    169    193       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      115    251       Fatty acid hydroxylase.
FT                                {ECO:0000259|Pfam:PF04116}.
SQ   SEQUENCE   297 AA;  34070 MW;  6EE13A09B0A2D989 CRC64;
     MSCIAGLFGS AAQRSAGSAW LLFAGCGVLQ VALSYLFCTP LERFWPLLRW PVRQPMATDI
     VYTFIVRIVL FPLAAYFEYG LVKALVERWL LAHQWPVPSL LTRIADVAGT PLAGFLIGFV
     ILDCADYWRH RISHRLGWWY GLHTLHHAEL QMTFWSDDRS HLLEDIITYV WLFVVAIAIG
     MPALQFPFVI LGFRFVGSFA HANTRARYGW LGERLLISPQ FHRAHHCPEI ARRKSCNFGT
     VLPWWDMLFG TANFTHDARE TGDPTADQII ATGNWWQQHV GGVRRMIQLA RRRRPAH
//

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