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Database: UniProt
Entry: A0A0M2JVF2_9MYCO
LinkDB: A0A0M2JVF2_9MYCO
Original site: A0A0M2JVF2_9MYCO 
ID   A0A0M2JVF2_9MYCO        Unreviewed;       379 AA.
AC   A0A0M2JVF2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KKF01044.1};
GN   ORFNames=WN67_15690 {ECO:0000313|EMBL:KKF01044.1};
OS   Mycolicibacterium obuense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF01044.1, ECO:0000313|Proteomes:UP000034150};
RN   [1] {ECO:0000313|EMBL:KKF01044.1, ECO:0000313|Proteomes:UP000034150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|EMBL:KKF01044.1,
RC   ECO:0000313|Proteomes:UP000034150};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium obuense UC1.";
RL   Submitted (APR-2015) 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:KKF01044.1}.
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DR   EMBL; LAUZ02000001; KKF01044.1; -; Genomic_DNA.
DR   RefSeq; WP_046363970.1; NZ_LAUZ02000001.1.
DR   AlphaFoldDB; A0A0M2JVF2; -.
DR   STRING; 1807.MOBUDSM44075_04399; -.
DR   PATRIC; fig|1807.13.peg.124; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000034150; 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; ISOVALERYL-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; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|RuleBase:RU362125}.
FT   DOMAIN          9..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          124..215
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;  40579 MW;  92FBD6B246832C19 CRC64;
     MPVDRLLPTD EAHELIELAR TIADKVLDPV VDQHEKDESY PDGVFTTLGE AGLLSLPYPE
     EWGGGGQPYE VYLQVLEELA ARWAAVAVAV SVHGLSCHPL MTFGSDEQRS RWLPDMLGGS
     TIGAYSLSEP QAGSDAAALT CRASAADGGY RITGEKAWIT HGGVADFYTL FARTGEGSQG
     ISCFLVPGDL DGLTFGRPEE KMGLHAVPTT AAHYDGAFLE EQRRIGAEGQ GLQIAFSALD
     AGRLGIAAVA VGLAQAALDA AVAYSQERTT FGRKIIDHQG LAFLLADMAA AVDSARATYL
     DAARRRDAGL TYSRQASVAK LVATDAAMKV TTDAVQVLGG AGYTRDYRVE RFMREAKITQ
     IFEGTNQIQR LVISRHLSR
//
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