(data stored in SCRATCH zone)

SWISSPROT: Q13HG2_PARXL

ID   Q13HG2_PARXL            Unreviewed;       415 AA.
AC   Q13HG2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   SubName: Full=Putative FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ABE36477.1};
DE            EC=1.18.1.3 {ECO:0000313|EMBL:ABE36477.1};
GN   ORFNames=Bxe_C0579 {ECO:0000313|EMBL:ABE36477.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36477.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36477.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36477.1,
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; ABE36477.1; -; Genomic_DNA.
DR   RefSeq; WP_011493733.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0579; -.
DR   EnsemblBacteria; ABE36477; ABE36477; Bxe_C0579.
DR   GeneID; 4010093; -.
DR   KEGG; bxb:DR64_7867; -.
DR   KEGG; bxe:Bxe_C0579; -.
DR   PATRIC; fig|266265.5.peg.8338; -.
DR   eggNOG; ENOG4108EQM; Bacteria.
DR   eggNOG; COG0446; LUCA.
DR   HOGENOM; HOG000276711; -.
DR   KO; K00529; -.
DR   OMA; GFDRQWS; -.
DR   OrthoDB; 1149616at2; -.
DR   BioCyc; BXEN266265:BXE_RS39410-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   4: Predicted;
DR   PRODOM; Q13HG2.
DR   SWISS-2DPAGE; Q13HG2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE36477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        5    302       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      321    403       Reductase_C. {ECO:0000259|Pfam:PF14759}.
SQ   SEQUENCE   415 AA;  43939 MW;  D95ECCA81521CC46 CRC64;
     MSVQHLVIVG AGQAGFQTAA SLRQAGFTGG IALVGDEPGV PYQRPPLSKA YLLGKIGTAA
     LRFRPDEWFD QQHVERLQAT VAAIDRDARC VVLADGARLA YDHLVLATGA RNRVPSVDGI
     ELDGVFGIRT LADADALSSR VDAARNVVVI GAGFIGLEFA AVAAAKGLSV RVIELGQRPM
     ARALSEPMSA LFGDAHRSWG VVFDFGQTVT RFIGKDGKVT AVETGSGEWV PADLVVYGIG
     VLPNTEIAAA AGLCVDNGIC VDEQLVTSDP AISAIGDAVS FPCAWSATRV RLESVQNAVD
     QARAVAARLV GTPAPYNALP WFWSDQGDLK LQIAGLSGGH DEAVVIGSIE QRQFSVLCFR
     EDRLIAVESC NRATDHMAAR KLLARGTALR VADARTPGFD FRAYESSSRD VPVCQ
//

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