ID A0A150XFF1_9BACT Unreviewed; 379 AA.
AC A0A150XFF1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KYG77433.1};
GN ORFNames=AWW68_01285 {ECO:0000313|EMBL:KYG77433.1};
OS Roseivirga spongicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG77433.1, ECO:0000313|Proteomes:UP000075606};
RN [1] {ECO:0000313|EMBL:KYG77433.1, ECO:0000313|Proteomes:UP000075606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG77433.1,
RC ECO:0000313|Proteomes:UP000075606};
RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL Submitted (JAN-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:KYG77433.1}.
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DR EMBL; LRPC01000001; KYG77433.1; -; Genomic_DNA.
DR RefSeq; WP_068215760.1; NZ_LRPC01000001.1.
DR AlphaFoldDB; A0A150XFF1; -.
DR STRING; 333140.AWW68_01285; -.
DR OrthoDB; 9764422at2; -.
DR Proteomes; UP000075606; 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 CDD; cd01158; SCAD_SBCAD; 1.
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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000075606}.
FT DOMAIN 6..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 231..378
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 379 AA; 41614 MW; 154E96204CDDB488 CRC64;
MNFELTEEQI AVRDAAREFA QTELLPGVIE RDDKQEFPAE QIKKMGELGF MGMMVDPKYG
GGGMDTVSYV LAMEEISKID ASASVCMSVN NSLVCWGLEK FGTEEQKEKY LKPLASGEKI
GAFCLSEPEA GSDATSQKTT AEDKGDHYLL NGTKNWITNG NSASIYLVIA QTDREKGHKG
INCLIVEKGM DGFVVGKKED KLGIRGSDTH SLMFTDVKVP KENRIGEDGF GFKFAMSTLN
GGRIGIASQA LGIASGAYEL ALAYSKERKA FGKPISQHQA IQFKLADMAT EIDAARLLCL
QAAYLKDQKK DFGKQSAMAK LYASKVAMDV TVEAVQVHGG YGYVKEYHVE RLMRDAKITQ
IYEGTSEIQK IVISRELLK
//
