(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKD5_PSEAB

ID   A0A0H2ZKD5_PSEAB        Unreviewed;       592 AA.
AC   A0A0H2ZKD5;
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:ABJ15470.1};
GN   OrderedLocusNames=PA14_06640 {ECO:0000313|EMBL:ABJ15470.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15470.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15470.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15470.1,
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; ABJ15470.1; -; Genomic_DNA.
DR   RefSeq; WP_003084848.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15470; ABJ15470; PA14_06640.
DR   KEGG; pau:PA14_06640; -.
DR   OMA; APLADMR; -.
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; A0A0H2ZKD5.
DR   SWISS-2DPAGE; A0A0H2ZKD5.
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        3     34       AcylCoA_DH_N. {ECO:0000259|Pfam:PF12418}.
FT   DOMAIN       39    158       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      163    272       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      283    452       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
FT   DOMAIN      468    585       Acyl-CoA_dh_C. {ECO:0000259|Pfam:
FT                                PF12806}.
SQ   SEQUENCE   592 AA;  63601 MW;  EDB1264F1A04E166 CRC64;
     MADYKAPLRD MRFVLNEVFE VSRLWAQLPA LAEVVDAETA AAILEEAGKV TAGTIAPLNR
     PGDEEGCQWN AGAVSTPAGF PEAYRTYAEG GWVGVGGDPA YGGMGMPKVI SAQVEELVNS
     ANLSFGLYPM LTAGACLALN AHASDELKDK YLPNMYAGIW AGSMCLTEPH AGTDLGIIRT
     KAEPQADGSY KISGTKIFIT GGEHDLTENI IHLVLAKLPD APAGPKGISL FLVPKVLVNA
     DGSLGEKNSL GCGSIEHKMG IKASATCVMN FDGATGWLVG EVNKGLAAMF TMMNYERLGV
     GIQGLATGER SYQSAIEYAR ERIQSRAPTG PVAKDKAADP IIVHPDVRRM LLTMKALNEG
     GRAFSSYVAM QLDTAKYSED AVTRKRAEEL VALLTPVAKA FLTDMGLETT IHGQQIFGGH
     GFIREWGQEQ LVRDCRITQI YEGTNGIQAL DLVGRKVIGS GGAFSRHFTD EIKAFVASAD
     EALGEFSKPL AAAVENLEEL TAWLLDRAKG NPNEIGAASV EYLHVFGYTA YAYMWALMAR
     TALAKQGEDD FYASKLGTAR FYFARLLPRI HSLSASVRAG SESLYLLDAE QF
//

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