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Database: UniProt
Entry: A0A3N0CRB4_9ACTN
LinkDB: A0A3N0CRB4_9ACTN
Original site: A0A3N0CRB4_9ACTN 
ID   A0A3N0CRB4_9ACTN        Unreviewed;       379 AA.
AC   A0A3N0CRB4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RNL65453.1};
GN   ORFNames=EFK50_05745 {ECO:0000313|EMBL:RNL65453.1};
OS   Nocardioides marmoriginsengisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=661483 {ECO:0000313|EMBL:RNL65453.1, ECO:0000313|Proteomes:UP000267128};
RN   [1] {ECO:0000313|EMBL:RNL65453.1, ECO:0000313|Proteomes:UP000267128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gsoil 097 {ECO:0000313|EMBL:RNL65453.1,
RC   ECO:0000313|Proteomes:UP000267128};
RA   Li F.;
RL   Submitted (NOV-2018) 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:RNL65453.1}.
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DR   EMBL; RJSE01000003; RNL65453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N0CRB4; -.
DR   OrthoDB; 142556at2; -.
DR   Proteomes; UP000267128; 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; 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   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:UP000267128}.
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          229..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  41865 MW;  A6B068A0164D4FE6 CRC64;
     MRDIFTAEHE DFRKTVRAFM EKEVVPFHDQ WDKDGIVPRE LWKKAGETGL LCFDVPEEFG
     GPGVDDFRYN VIVSEEQTRA NVSGPGFSVH TDIIVPYLIS IANDEQKARW LPGCVSGDTI
     TAIAMTEPGA GSDLQGIRTT AIDKGDHYLV NGSKTFISNG IHADLVIVVA RTDPDAGHKG
     ISLIVLEEGM EGFERGRNLD KIGLHAQDTA ELSFTDVMVP KENLLGEEGQ GFIYLMMNLP
     QERLIIAAQA VAACEAVLDM CLEYAKTREA FGKPIGKFQH NRFLLAEMAT ETKIARVFID
     DCLKKHLAGK LDAVDASMAK YHATELQNKH VNQGVQLHGG YGYMLEYPIA KAYLDSRIST
     IYGGTTEIQK EIIGRSLGI
//
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