ID A0A0Q5YB97_9BRAD Unreviewed; 397 AA.
AC A0A0Q5YB97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG57_15260 {ECO:0000313|EMBL:KQT02948.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT02948.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT02948.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT02948.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT02948.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT02948.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT02948.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMQJ01000066; KQT02948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5YB97; -.
DR Proteomes; UP000051536; 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; 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}.
FT DOMAIN 11..125
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..216
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 244..393
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 397 AA; 44686 MW; F1C8DE6FAE3A0F7B CRC64;
MEIAVDFELS REQQDIKARA AAFVDEVCRP LEDRWGTDDY AVPHDIFMDV VRKFREYGFR
GIAVPKEAGG QGLGTIAKCL VYEEIVRSPV MHGLLATWSG FLDPHPALYV APEWQREAYL
YPILKEDKFY HINISEPGAG SDAAGIQTTA VRVGDSYVIN GIKRWAPPPN HPGITPKYLL
CYAVTDPGKG YEGISLFLVD YPNPGVSVLR EYETMAPGTY LGRSCDYQYK DCVVPARNML
GQEGMGFRYM MDQLNRNRTV IGARLTGTAR WAQGEAAKRA RERETFGKPL AERQAIQWML
AESEMDLEQS RLMVYKTAWM LDRGMDARKE AAMVKCFAPL AACRVIDRAI QIHGGLGVLR
ENRFGQLYFQ SRIAQVAEGT TEVMKMTIAR EVLRATD
//
