ID A0A1X7EKY6_9PROT Unreviewed; 386 AA.
AC A0A1X7EKY6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SMF35799.1};
GN ORFNames=SAMN02982917_1836 {ECO:0000313|EMBL:SMF35799.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF35799.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF35799.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF35799.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FXAK01000002; SMF35799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7EKY6; -.
DR STRING; 286727.SAMN02982917_1836; -.
DR OrthoDB; 5510711at2; -.
DR Proteomes; UP000192936; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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 13..125
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 129..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 242..383
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42118 MW; BB496AEA76844B08 CRC64;
MHNIVFPPPP VTARTEALRA EVRDFLKTEL ADRPPRLRAD SWNGFDAGFS RKMGERGWIG
MTWPTRYGGH ERSALERYVV LEEVLAAGAP VAAHWIADRQ SGPLLLKNGT EEQRQRILPR
IAAGDCTFCI GMSEPDSGSD LAAVRTRAVP VQGGGGGGWR VNGTKLWTTY AHHAHYMILF
CRTDGGTEDR QGGTSQFLVD LKTPGITIRP VLDMTGAHHF NEVVFEDALL PDDALIGQRG
EGWAQVMGEL AYERSGPERF LSSMTLLTEL VRALGDAPSD QAAMAVGRLT AHLLVLRRLS
RSVAGMLENG ENPALQAALV KDLGALFEQE IPEIARQLVN AEPDLQATRE FSAVLAKLVM
NAPSFSLRGG TREILRGIIA RGLGLR
//
