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Database: UniProt
Entry: A0A0M2CZL0_9MICC
LinkDB: A0A0M2CZL0_9MICC
Original site: A0A0M2CZL0_9MICC 
ID   A0A0M2CZL0_9MICC        Unreviewed;       392 AA.
AC   A0A0M2CZL0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EYT55606.1};
GN   ORFNames=H488_0100495 {ECO:0000313|EMBL:EYT55606.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT55606.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT55606.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT55606.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(2013).
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:EYT55606.1}.
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DR   EMBL; AOSQ01000001; EYT55606.1; -; Genomic_DNA.
DR   RefSeq; WP_017831811.1; NZ_AOSQ01000001.1.
DR   AlphaFoldDB; A0A0M2CZL0; -.
DR   HOGENOM; CLU_018204_8_0_11; -.
DR   Proteomes; UP000033173; 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; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42807:SF1; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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          17..127
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          131..226
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          239..385
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   392 AA;  42390 MW;  F54C97BC65BFD4B5 CRC64;
     MNAAATDLLD VEADLSAEEL ETRDTVREFV DRRIRPNIAG WFADAVFPQE IVPEMAQLGL
     LGMHIQGYGC AGKSAVQYGI AMQELEAGDS GLRTFVSVQG SLAMSAIAKH GSEEQKQRWL
     PGMAAGEIIG CFGLTEPTAG SDPSTMATTA VREGGEWVLN GAKRWIGLAS IAHVAVIWAK
     AVDESGQERV RGFLVPTDTP GFTATPIEPK LSMRASIQCD IALEDVRLPA DAILPDNPGL
     RGPFSCLNEA RYGIVWGALG AARDSFDAAL AYSQQRIQFD KPLAAYQLSQ AKLVNMALEI
     QKGQLLALRI GRLKDEGRLE NHMISVGKLN NCRIAIEVCR EARTMLGGNG VTLEHSPLRH
     ANNLESVRTY EGTDEVHTLI LGQQLTGHSA FR
//
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