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Database: UniProt
Entry: A0A1V2GVC7_9PROT
LinkDB: A0A1V2GVC7_9PROT
Original site: A0A1V2GVC7_9PROT 
ID   A0A1V2GVC7_9PROT        Unreviewed;       413 AA.
AC   A0A1V2GVC7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ONG46547.1};
GN   ORFNames=BKE38_25210 {ECO:0000313|EMBL:ONG46547.1};
OS   Pseudoroseomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG46547.1, ECO:0000313|Proteomes:UP000188879};
RN   [1] {ECO:0000313|EMBL:ONG46547.1, ECO:0000313|Proteomes:UP000188879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3 {ECO:0000313|EMBL:ONG46547.1,
RC   ECO:0000313|Proteomes:UP000188879};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Roseomonas sp. strain M3.";
RL   Submitted (OCT-2016) 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:ONG46547.1}.
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DR   EMBL; MLCO01000316; ONG46547.1; -; Genomic_DNA.
DR   RefSeq; WP_076960046.1; NZ_MLCO01000316.1.
DR   AlphaFoldDB; A0A1V2GVC7; -.
DR   OrthoDB; 5510711at2; -.
DR   Proteomes; UP000188879; 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:UP000188879}.
FT   DOMAIN          11..129
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..235
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          247..395
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   413 AA;  46063 MW;  CABE2875262B8015 CRC64;
     MDFSYSPKVV ALRERLQAFM DEHIIPNDHL HHEQHAAMPD RWQPVPIVET LKPKAREAGL
     WNLFLPASHH GAGLTNLEYA PLAEIMGAYP WASEVFNCSA PDTGNMETIE RYGTEAHKAR
     WLTPLLAGEI RSCFAMTEPD VASSDATNIQ TRITRDGDHY VINGRKWWSS GAGDPRCQVF
     IVMGKTDPDS PDKHRQQSMI LVPRDAPGLV IKRMLPVFGF DDAPHGHAEL LFNDVRVPVD
     NILLGEGRGF EIAQGRLGPG RIHHCMRAIG LAERALAMMC KRALERRPFG KPLADQGVMV
     DRIAQSRILI DQCRLLTLHA AWRMDTVGNK VARTEIAEIK VAAPDMACQV IDWAIQAHGG
     GGVTEDFPLA YMYKIARTLR IVDGPDEVHR FQLGRMELNK HRPPRNAGVG QGV
//
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