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Database: UniProt
Entry: W9TRG1_9PSED
LinkDB: W9TRG1_9PSED
Original site: W9TRG1_9PSED 
ID   W9TRG1_9PSED            Unreviewed;       416 AA.
AC   W9TRG1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EXF45389.1};
GN   ORFNames=BAY1663_02158 {ECO:0000313|EMBL:EXF45389.1};
OS   Pseudomonas sp. BAY1663.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF45389.1, ECO:0000313|Proteomes:UP000019475};
RN   [1] {ECO:0000313|EMBL:EXF45389.1, ECO:0000313|Proteomes:UP000019475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAY1663 {ECO:0000313|EMBL:EXF45389.1,
RC   ECO:0000313|Proteomes:UP000019475};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of Pseudomonas sp. BAY1663.";
RL   Submitted (DEC-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF45389.1}.
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DR   EMBL; AZSV01000025; EXF45389.1; -; Genomic_DNA.
DR   RefSeq; WP_037039903.1; NZ_AZSV01000025.1.
DR   AlphaFoldDB; W9TRG1; -.
DR   STRING; 1439940.BAY1663_02158; -.
DR   PATRIC; fig|1439940.3.peg.2148; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000019475; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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   Reference proteome {ECO:0000313|Proteomes:UP000019475}.
FT   DOMAIN          9..129
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..216
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          245..394
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   416 AA;  46694 MW;  305D81E08FA58CE6 CRC64;
     MNFAYSPRVE ALRQQLRAFM EQYIVPRIGA WHAEVGAGRY PISFMEDLKA LARSEGLWNL
     FLPSLREDEP GMGLSNLEYA PLAEIMGRVH WASEVFNCNA PDTGNMELLH LFATPEQRQR
     WLKPLLEGEI RSAFAMTEPD VPSSDATNIQ TLIQRDGDDY VINGRKWFIT NASHPNCKLL
     IVMGKTDPQA DTHHQQSMIL VPFDTPGVEL LRNIPVMNHI APEGHSELLL RNVRVPASNL
     LGREGDGFMM AQARLGPGRI HHCMRSIGMA ELALELMVER CQERKAFGKY LQQYSNIGDW
     IAESRIEIEQ ARLLVLKTAW MIDEVGAKAA RKEIAMIKAL VPRMHTRVVD RAIQVYGAMG
     LTPDTPLADM WTGGRALRFA DGPDQVHLRS IARMELKASE ASRGATAAYL TPPGRH
//
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