UniProt: A0A0W0R4B3

Database: UniProt
Entry: A0A0W0R4B3_9GAMM

LinkDB:  A0A0W0R4B3_9GAMM 
Original site:  A0A0W0R4B3_9GAMM

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
All databases (20)   

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ID   A0A0W0R4B3_9GAMM        Unreviewed;       385 AA.
AC   A0A0W0R4B3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Acyl CoA dehydrogenase {ECO:0000313|EMBL:KTC65901.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:VEH85521.1};
GN   Name=acdA {ECO:0000313|EMBL:KTC65901.1};
GN   ORFNames=Lade_0559 {ECO:0000313|EMBL:KTC65901.1}, NCTC12735_01155
GN   {ECO:0000313|EMBL:VEH85521.1};
OS   Legionella adelaidensis.
OG   Plasmid 18 {ECO:0000313|EMBL:VEH85521.1,
OG   ECO:0000313|Proteomes:UP000281170}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC65901.1, ECO:0000313|Proteomes:UP000054859};
RN   [1] {ECO:0000313|EMBL:KTC65901.1, ECO:0000313|Proteomes:UP000054859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC65901.1,
RC   ECO:0000313|Proteomes:UP000054859};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Identification of large and diverse effector repertoires of 38 Legionella
RT   species.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VEH85521.1, ECO:0000313|Proteomes:UP000281170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH85521.1,
RC   ECO:0000313|Proteomes:UP000281170};
RC   PLASMID=18 {ECO:0000313|Proteomes:UP000281170};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; LNKA01000001; KTC65901.1; -; Genomic_DNA.
DR   EMBL; LR134427; VEH85521.1; -; Genomic_DNA.
DR   RefSeq; WP_058461624.1; NZ_LR134427.1.
DR   AlphaFoldDB; A0A0W0R4B3; -.
DR   STRING; 45056.Lade_0559; -.
DR   KEGG; ladl:NCTC12735_01155; -.
DR   PATRIC; fig|45056.6.peg.580; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000054859; Unassembled WGS sequence.
DR   Proteomes; UP000281170; Plasmid 18.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
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   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:VEH85521.1}; Plasmid {ECO:0000313|EMBL:VEH85521.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054859}.
FT   DOMAIN          6..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  42959 MW;  0DD63F7147AC20C5 CRC64;
     MDFQLSEENR AFRQMAADFA RDKIQPYADS WDEDHHFPVE VFKQAAQLGM GGIVANEDIG
     GAGLPRLASA LIFEQLATGC VSTSAYLSIH NMVVSLIDRY GSDELRRVWG PKLTSMDVLA
     SYCLTEPESG SDAASLRTTA KREGDYYLVN GTKAFISGAG VSDVYLCMVR TGNEKHHGIT
     SLLIEKDTLG LSFGKLEKKM GWRNQPTAMI YFENCRVPVK NRVGDEGQGF KIALNALNGG
     RVSIAACALG GALSCLRLTQ SYMHERKQFG KALKEMQGLR FYFADMLTNF DAARLMVYRA
     ADSLDRNNAK APMYCAMAKQ LATDFAFAIS DKAMQLHGGY GYLRDYQIER IFRDLRVHQI
     LEGTNEIMRE IIAKSVLDDE KYFLE
//

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