(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKQ6_PSEAB

ID   A0A0H2ZKQ6_PSEAB        Unreviewed;       598 AA.
AC   A0A0H2ZKQ6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:ABJ15469.1};
GN   OrderedLocusNames=PA14_06620 {ECO:0000313|EMBL:ABJ15469.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15469.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15469.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15469.1,
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).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000438; ABJ15469.1; -; Genomic_DNA.
DR   RefSeq; WP_003137312.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15469; ABJ15469; PA14_06620.
DR   KEGG; pau:PA14_06620; -.
DR   OMA; HEWGMEQ; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_DH_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZKQ6.
DR   SWISS-2DPAGE; A0A0H2ZKQ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN        4     29       AcylCoA_DH_N. {ECO:0000259|Pfam:PF12418}.
FT   DOMAIN       39    156       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      162    270       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      281    450       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
FT   DOMAIN      468    591       Acyl-CoA_dh_C. {ECO:0000259|Pfam:
FT                                PF12806}.
SQ   SEQUENCE   598 AA;  64366 MW;  FCCF782CC1D8AF25 CRC64;
     MPEYKAPLRD MRFLIDEVFD FHGRYQALGA SDATPDMVAA ILDEGSKFCE QVLAPLNRSG
     DEEGCHFDNG VVTTPKGFKE AYAQYVEGGW NGVASDPAYG GQGLPHSLGL LLSEMIGSSN
     VSWGMYPGLT RGAMSAIHAH GSQAQKDLYL ARMTAGTWTG TMCLTEPHCG TDLGIIKTRA
     VPNADGSHAI SGTKIFISAG EHDLSENIVH LVLAKLPDAP AGTKGISLFI VPKFLPDAEG
     NVGARNAVSC GSIEHKMGIK ASATCVMNFD GATGYLIGEP NKGLHCMFTM MNHARLGTGM
     QGLCLGETSY QGAVRYARER LQMRSLTGPK APDKPADPII VHPDVRRMLL TMKAFNEGNR
     ALAYFTAQLL DTEHLSQDAA ERERAADLLA FLTPICKAFM TETGQEVTNL GMQVYGGHGY
     IREWGMEQLV RDCRIAQIYE GTNGIQALDL LGRKVLGSQG KLLRGFTKLV HQLCQAQAEH
     PQLKGQVAQL AALNAQWGEL TQQVGLAAMK NADEVGAASV DYLMFSGYVT LAYFWLRIAL
     VAREKLDAGS GEAAFYEAKL ATADFYFSRL LPRTAAHAAA IQAGAAGLMS LSAEQFSL
//

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