ID A0A0M3U886_9PSEU Unreviewed; 387 AA.
AC A0A0M3U886;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALE78389.1};
GN ORFNames=WY02_08045 {ECO:0000313|EMBL:ALE78389.1};
OS Pseudonocardia sp. AL041005-10.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE78389.1, ECO:0000313|Proteomes:UP000067245};
RN [1] {ECO:0000313|EMBL:ALE78389.1, ECO:0000313|Proteomes:UP000067245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE78389.1,
RC ECO:0000313|Proteomes:UP000067245};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(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; CP011862; ALE78389.1; -; Genomic_DNA.
DR RefSeq; WP_062403475.1; NZ_CP011862.1.
DR AlphaFoldDB; A0A0M3U886; -.
DR STRING; 445576.WY02_08045; -.
DR KEGG; psea:WY02_08045; -.
DR PATRIC; fig|445576.3.peg.1795; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000067245; Chromosome.
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 CDD; cd00567; ACAD; 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; 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:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 1.
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 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.
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 9..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 232..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 387 AA; 41234 MW; CE705D2B8EDD2929 CRC64;
MQDDLLVDTD ERRALREAVA KLVGAYGRSY FQEVTRSGGR PDDLWADLGR AGYLGVHLPE
EHGGGGGGLT DLAIVIEETA AQGCPLFMLV ISPAIAGSLL VAHASDEQKR TWLPGVADGT
KRIAFAITEP DAGTNTHNIT TTAHPDGDGW RIRGQKYWTS GIDDADAVIV VCRGAEAGPD
GRHPISMFLV PTDAPGLSFT RIDAALQIPE NQFTTFFDDV RVTRDDLIGV EGAGLRQVFA
GLNPERVTAA AQANGIARYA LRRAARYAAE RTVWSTPIGA HQGVAHPLAA CFVDVQLARL
MTMHAAELTD AGADAGSAST VAKYAAGEAA AKAVDQAIQT HGGNGLSNEY GLADLWFTAR
MFRTAPVSRE MVLNHVAQYN LDLPKSY
//
