(data stored in SCRATCH zone)

SWISSPROT: Q145G7_PARXL

ID   Q145G7_PARXL            Unreviewed;       471 AA.
AC   Q145G7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=Putative FAD-binding oxidase {ECO:0000313|EMBL:ABE29022.1};
DE            EC=1.1.2.4 {ECO:0000313|EMBL:ABE29022.1};
GN   ORFNames=Bxe_A3977 {ECO:0000313|EMBL:ABE29022.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29022.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29022.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29022.1,
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; ABE29022.1; -; Genomic_DNA.
DR   RefSeq; WP_011486845.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3977; -.
DR   EnsemblBacteria; ABE29022; ABE29022; Bxe_A3977.
DR   GeneID; 4004616; -.
DR   KEGG; bxb:DR64_1653; -.
DR   KEGG; bxe:Bxe_A3977; -.
DR   PATRIC; fig|266265.5.peg.512; -.
DR   eggNOG; ENOG4105CQB; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230995; -.
DR   KO; K00102; -.
DR   OMA; GQGFEWA; -.
DR   OrthoDB; 1188552at2; -.
DR   BioCyc; BXEN266265:BXE_RS02425-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
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; Q145G7.
DR   SWISS-2DPAGE; Q145G7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE29022.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       48    225       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   471 AA;  51090 MW;  B6677E861084033C CRC64;
     MNHPVPPAPL RRPFPAELLS ALKAAFAERV SVSEAVRVHH GRDESPFDPQ LPDAVVFART
     TEDVQNVVKL CGQYNVPVIP YGNGSSLEGH LLAVQGGVSI DLSEMNRVLS INAEDLTVTV
     EPGISRKQLN EALRDTGLFF PIDPGADASI GGMSATRASG TNAVRYGTMR ENVLGLTVVL
     ADGRVIKTGT RARKSSAGYD LTRLFVGSEG TLGVITEITV RLYPQPEAVS AAVCTFPSMG
     DAVRAVIETI QIGVPIARVE FVDSLAIRSI NRHSNLTLRE APTLFFEFHG TEAGVKEQAE
     LVQEVAAQNA GEGFEWATRP EDRSRLWNAR HNAYFAMLQL KPGCRAVTTD VCVPISRLAE
     CVEETEQDLK ASPLPCPIVG HVGDGNFHVA ILIDPNKPEE LVEAERLNHR IVERALRMDG
     TCTGEHGVGL HKMGFLLEEH GEVAVDTMRS IKHALDPHNL MNPGKIFSWA A
//

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