(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJW5_PSEAB

ID   A0A0H2ZJW5_PSEAB        Unreviewed;       464 AA.
AC   A0A0H2ZJW5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   SubName: Full=Putative oxidoreductase, FAD-binding {ECO:0000313|EMBL:ABJ15280.1};
GN   OrderedLocusNames=PA14_04140 {ECO:0000313|EMBL:ABJ15280.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15280.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15280.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15280.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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DR   EMBL; CP000438; ABJ15280.1; -; Genomic_DNA.
DR   RefSeq; WP_003084351.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15280; ABJ15280; PA14_04140.
DR   KEGG; pau:PA14_04140; -.
DR   OMA; WSTIGGN; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
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; A0A0H2ZJW5.
DR   SWISS-2DPAGE; A0A0H2ZJW5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653}.
FT   DOMAIN       37    216       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   464 AA;  51315 MW;  17F1D060AE8B8FA2 CRC64;
     MTREALIESL KPLVEPGKLL DDAASLDAYG KDWTKHFAPA PLAIVFPKSV EQVQAIVRWA
     NQHKVGLVPS GGRTGLSAAA VAANGEVVVA FDYMNRILDF NAFDRTVVCQ PGVVTKQLQT
     FAEENGLYYP VDFASSGSSQ IGGNIGTNAG GIKVIRYGMT RNWVAGMKVV TGKGDLLELN
     KDLIKNATGY DMRQLFIGAE GTLGFVVEAT MRLERTPKNL TAMVLGTPDF DSIMPVLHAF
     QSKLDLTAFE FFSDKALAKV LARGDVPRAF ETDCPFYALL EFEATTEEVA NEALATFEHC
     VEQGWVLDGV MSQSEQQLQN LWKLREYISE TISHWTPYKN DISVTVSRVP AFLKDIDAIV
     EANYPDFEVV WFGHIGDGNL HLNILKPENL GKDEFFARCA TVNKWVFETV EKYNGSISAE
     HGVGMTKRDY LTYTRSETEI AYMKALKAVF DPNGIMNPGK IFAE
//

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