(data stored in ACNUC7421 zone)

SWISSPROT: Q145G9_PARXL

ID   Q145G9_PARXL            Unreviewed;       362 AA.
AC   Q145G9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Putative glycolate oxidase, subunit GlcE {ECO:0000313|EMBL:ABE29020.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:ABE29020.1};
GN   ORFNames=Bxe_A3979 {ECO:0000313|EMBL:ABE29020.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29020.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29020.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29020.1,
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; CP000270; ABE29020.1; -; Genomic_DNA.
DR   RefSeq; WP_011486843.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3979; -.
DR   EnsemblBacteria; ABE29020; ABE29020; Bxe_A3979.
DR   GeneID; 4004614; -.
DR   KEGG; bxb:DR64_1655; -.
DR   KEGG; bxe:Bxe_A3979; -.
DR   PATRIC; fig|266265.5.peg.510; -.
DR   eggNOG; ENOG4105EU8; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230994; -.
DR   KO; K11472; -.
DR   OMA; WGTLAVM; -.
DR   OrthoDB; 295054at2; -.
DR   BioCyc; BXEN266265:BXE_RS02415-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; Q145G9.
DR   SWISS-2DPAGE; Q145G9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00999659,
KW   ECO:0000313|EMBL:ABE29020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        1    172       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   362 AA;  38793 MW;  827954FF741A5659 CRC64;
     MEEDDIVAGW SERVRSASAE GRALRIRGGG TKDWYGQTLE GDILDTRAYR GIIAYDPAEL
     VITARAGTPL LEIEAALADH HQMLAFEPPH FGPQATFGGC IAAGIAGPRR PSAGAARDFV
     LGAVIMNGQG QTLHFGGQVV KNVAGYDVSR LMAGSLGTLG LILELSIKVL PLPQAEATLK
     FDMNGTDAVR KLNEWGGRPL PITASAWRHG TLAVRLAGAE AAVKSARTSL GGEVVDAVEA
     ERFWAGLREQ TDSFFSAIPP KAALWRLALP SITEPLQLPG AQLMEWGGGQ RWWITDTDAQ
     TVRISAKQAG GHATIFRTGH GYDRGAGVFT PLPAPLMKIH RGLKAAFDPA RIFNRGRLYP
     DF
//

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