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Database: UniProt
Entry: A0A0U4CKX7_9ACTN
LinkDB: A0A0U4CKX7_9ACTN
Original site: A0A0U4CKX7_9ACTN 
ID   A0A0U4CKX7_9ACTN        Unreviewed;       408 AA.
AC   A0A0U4CKX7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALX03356.1};
GN   ORFNames=AERYTH_00890 {ECO:0000313|EMBL:ALX03356.1};
OS   Aeromicrobium erythreum.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX03356.1, ECO:0000313|Proteomes:UP000067689};
RN   [1] {ECO:0000313|EMBL:ALX03356.1, ECO:0000313|Proteomes:UP000067689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR18 {ECO:0000313|EMBL:ALX03356.1,
RC   ECO:0000313|Proteomes:UP000067689};
RX   PubMed=1883712;
RA   Miller E.S., Woese C.R., Brenner S.;
RT   "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT   strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL   Int. J. Syst. Bacteriol. 41:363-368(1991).
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; CP011502; ALX03356.1; -; Genomic_DNA.
DR   RefSeq; WP_067853402.1; NZ_CP011502.1.
DR   AlphaFoldDB; A0A0U4CKX7; -.
DR   STRING; 2041.AERYTH_00890; -.
DR   KEGG; aer:AERYTH_00890; -.
DR   PATRIC; fig|2041.4.peg.184; -.
DR   OrthoDB; 142556at2; -.
DR   Proteomes; UP000067689; 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   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:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067689}.
FT   DOMAIN          17..131
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          136..238
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          250..400
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   408 AA;  45164 MW;  CA43186FA0954506 CRC64;
     MHFAFDETTT ELIAKLEAFM DEAVYPAEAE AAEQIETLYA EDRWDPPAVL DGLKEQARER
     GLWNFFLAGH PEEGGLTNLQ YAPLAEITGR SIQLAPAALN CAAPDTGNME VLTMFGTPEQ
     KEQWLRPLLD GQIRSAFAMT EPDVASSDAT NIGLSIVRDG DEYVINGRKW WITGAMNPNC
     RVFIVMGKTD PSAERHRQQS MILVPRDTPG LEVVRGMHVF GYHDRDHGGH AELRFTDVRV
     PASNLIGGEG EGFAIAQARL GPGRIHHCMR SIGIAERAVE YMCERALSRT TFGKPIAQQG
     VVQDWIAESR VRLEQLRLLT LKTAWLMDTV GNRGAHKEIQ AIKIATPQTV EWILDKAIQV
     HGAGGLSQDF PLAEMFAGIR TLRFADGPDE VHKASLARAE LKKYAVRG
//
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