(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZL63_PSEAB

ID   A0A0H2ZL63_PSEAB        Unreviewed;       393 AA.
AC   A0A0H2ZL63;
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=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:ABJ15412.1};
GN   Name=gcdH {ECO:0000313|EMBL:ABJ15412.1};
GN   OrderedLocusNames=PA14_05840 {ECO:0000313|EMBL:ABJ15412.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15412.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15412.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15412.1,
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; ABJ15412.1; -; Genomic_DNA.
DR   RefSeq; WP_003084682.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZL63; -.
DR   SMR; A0A0H2ZL63; -.
DR   EnsemblBacteria; ABJ15412; ABJ15412; PA14_05840.
DR   KEGG; pau:PA14_05840; -.
DR   KO; K00252; -.
DR   OMA; TQTYEGQ; -.
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; IPR006089; Acyl-CoA_DH_CS.
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; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZL63.
DR   SWISS-2DPAGE; A0A0H2ZL63.
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       20    132       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      136    227       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      239    385       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   393 AA;  43311 MW;  174476ADE563ECD1 CRC64;
     MATKASFNWE DPLLLDQQLT EEERMVRDSA QQFAQDKLAP RVLEAFRHEQ TDPKIFREMG
     ETGLLGATIP EAYGGSGLNY VCYGLIAREV ERVDSGYRSM MSVQSSLVMV PIHEFGNEAT
     RQKYLPKLAS GEYIGCFGLT EPNHGSDPGS MVTRAKKVDG GYRLSGSKMW ITNSPIADVF
     VVWAKDDEGQ IRGFVLEKGW EGLSAPAIHG KVGLRASITG EIVMDNVFVP EENAFPEVRG
     LRGPFTCLNS ARYGISWGAL GAAEFCWHTA RQYVLDRQQF GRPLAANQLI QKKLADMQTE
     ITLALQGCLR LGRMKDEGTA AVEITSIMKR NSCGKALDIA RLARDMLGGN GISDEFGIAR
     HLVNLEVVNT YEGTHDVHAL ILGRAQTGIQ AFF
//

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