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Database: UniProt
Entry: A0A0R3MK10_9BRAD
LinkDB: A0A0R3MK10_9BRAD
Original site: A0A0R3MK10_9BRAD 
ID   A0A0R3MK10_9BRAD        Unreviewed;       384 AA.
AC   A0A0R3MK10;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRR20585.1};
GN   ORFNames=CQ14_11245 {ECO:0000313|EMBL:KRR20585.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR20585.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR20585.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR20585.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) 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:KRR20585.1}.
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DR   EMBL; LLYB01000086; KRR20585.1; -; Genomic_DNA.
DR   RefSeq; WP_057860396.1; NZ_LLYB01000086.1.
DR   AlphaFoldDB; A0A0R3MK10; -.
DR   STRING; 722472.SAMN05444321_2724; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000051660; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
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; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48083:SF6; ZGC:85777; 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; 1.
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}.
FT   DOMAIN          4..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..375
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  42283 MW;  0D2A4841C05AC214 CRC64;
     MLFTADHDEP RRILQKFIAA EINPFVDEWE KNDIFPAHEL FKKLGDLGFL GLNKPVEFGG
     QGLDYSYALM MAEELGAITC GGVPMAIGVQ TDMATPALAR FGSDEVRREF LSPAIAGDAV
     ACIGVSEPGA GSDVASIKTN ARADGDDYVI NGGKMWITNG VQADWICLLA NTSDDQVHRN
     KSLICVPMKS KGVQVARKLD KMGMRSSDTA QIFFDNVRVP KRNRIGEEGK GFTYQMVQFQ
     EERLWGAAAC LKAHEFIISE TIEYTRNRKA FGKSILDNQT VHFKLAEMQT EVELLRALIY
     RAAEALIAGE DVTRLATMAK LKAGRLGREL TDACLQFWGG MGFMNETPVS RAYRDSRLTS
     IGGGADEVML TVLCKMMGTL PKNQ
//
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