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Database: UniProt
Entry: A0A318KKI0_9NOCA
LinkDB: A0A318KKI0_9NOCA
Original site: A0A318KKI0_9NOCA 
ID   A0A318KKI0_9NOCA        Unreviewed;       390 AA.
AC   A0A318KKI0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:PXX68907.1};
GN   ORFNames=DFR70_102593 {ECO:0000313|EMBL:PXX68907.1};
OS   Nocardia tenerifensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=228006 {ECO:0000313|EMBL:PXX68907.1, ECO:0000313|Proteomes:UP000247569};
RN   [1] {ECO:0000313|EMBL:PXX68907.1, ECO:0000313|Proteomes:UP000247569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44704 {ECO:0000313|EMBL:PXX68907.1,
RC   ECO:0000313|Proteomes:UP000247569};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-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:PXX68907.1}.
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DR   EMBL; QJKF01000002; PXX68907.1; -; Genomic_DNA.
DR   RefSeq; WP_040738433.1; NZ_QJKF01000002.1.
DR   AlphaFoldDB; A0A318KKI0; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000247569; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          7..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..387
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   390 AA;  42993 MW;  E1829043A3BF4F24 CRC64;
     MKMSLSPDEV AFRDELRQIY RTEIPADIRE RFKYGQELSR DDIVRSHKAL NDHGLAVPNW
     PVEWGGKDWT PMQRHIWQDE MQLASVPDPL TFNAQMVGPV IAHFGSQELK ERFLPPTAAL
     DIWWCQGFSE PDAGSDLASL RTTAVRDGDS YIVNGQKIWT TLAQYADWIF CLVRTDPSAA
     KKQAGISFLL FDVKSPGVTI RPIKLIDGGY EVNEVFFENV RVPADQLVGE ENMGWTYAKF
     LLGNERTGIT GVGRTKVKLG IAKEYAAKTK SGEGTLLSDP LFAARIAELE NELLALELTQ
     LRVVSNSADG KPNPASSVLK LRGSELQQAA TELLVDIAGP DALPVGADEI ASPAWAQRSG
     PGYLNYRKTT IYGGSSEVQR TIIASTILGL
//
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