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Database: UniProt
Entry: A0A0S6UHN4_9BRAD
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Original site: A0A0S6UHN4_9BRAD 
ID   A0A0S6UHN4_9BRAD        Unreviewed;       389 AA.
AC   A0A0S6UHN4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAJ31018.1};
GN   ORFNames=BDOA9_0101910 {ECO:0000313|EMBL:GAJ31018.1};
OS   Bradyrhizobium sp. DOA9.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ31018.1};
RN   [1] {ECO:0000313|EMBL:GAJ31018.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOA9 {ECO:0000313|EMBL:GAJ31018.1};
RX   PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA   Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA   Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA   Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT   "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT   Plasmid.";
RL   PLoS ONE 10:e0117392-e0117392(2015).
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; DF820425; GAJ31018.1; -; Genomic_DNA.
DR   RefSeq; WP_025032074.1; NZ_DF820425.1.
DR   AlphaFoldDB; A0A0S6UHN4; -.
DR   STRING; 1126627.BDOA9_0101910; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000066441; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          7..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..221
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   389 AA;  42957 MW;  914BA0CD395E141B CRC64;
     MSQEHHTEDY ADIREAVAKL CAQFPGEYWR KLDREMAYPK AFVDALTEAG YLSVLIPEEY
     GGAGLKLSAA AAILEEIQRA GCNGGGCHAQ MYTMGTVLRH GNAEQKAKYL PKIASGELRL
     QAFGVTEPTS GTDTSSLKTF ARKDGNDSYI VNGQKIWTSR AEHSDLMVLL ARTTPKDQVK
     KRTDGLSVFI VDMREAKNNG LEIRPIRTMM NHATTEVFFT DMRVPAENLI GEEGKGFRYI
     LSGMNAERIL IAAECVGDAK WFIAKATTYA KERAVFGRPI GQNQGIQFPI AKAYASMRAA
     ELMVKEATRK YEAGLDCGAE ANMAKMLAAD ASWEAANACI QTHGGFGFAE EYDVERKFRE
     TRLYQVAPIS TNLVLSFVAE HVLGMPRSY
//
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