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Database: UniProt
Entry: A0A024QHP6_9BACI
LinkDB: A0A024QHP6_9BACI
Original site: A0A024QHP6_9BACI 
ID   A0A024QHP6_9BACI        Unreviewed;       393 AA.
AC   A0A024QHP6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CDQ42063.1};
GN   Name=mmgC_3 {ECO:0000313|EMBL:CDQ42063.1};
GN   ORFNames=BN990_04443 {ECO:0000313|EMBL:CDQ42063.1};
OS   Virgibacillus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ42063.1, ECO:0000313|Proteomes:UP000028875};
RN   [1] {ECO:0000313|EMBL:CDQ42063.1, ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ42063.1,
RC   ECO:0000313|Proteomes:UP000028875};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL   Submitted (MAY-2014) 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:CDQ42063.1}.
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DR   EMBL; CCDP010000004; CDQ42063.1; -; Genomic_DNA.
DR   RefSeq; WP_038247443.1; NZ_WMER01000004.1.
DR   AlphaFoldDB; A0A024QHP6; -.
DR   STRING; 1462526.BN990_04443; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000028875; 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; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028875}.
FT   DOMAIN          6..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..221
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          236..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   393 AA;  44472 MW;  65E2EF5717CA0DC2 CRC64;
     MDLRLSEEQR MVQKTIRKFV EKELMPLENE VLRNERNGMP SLSAEKQEEL QLKAKEAGFW
     GINTPTEYGG ADLGQMMQAI VTMEVSKTFV PFTFGGSADN ILYYGNEEQK KKYLIPTING
     EKKSCFAMTE PGAGSDTQNI KMTAVKDGNE WVLNGEKTFI TGGNEADFVM VIAITDKDMH
     QKTKGRDGVT CFIVDRNMGW KSEYIHTMGD WGPASLVFDN VRVPEENILG ELHAGGYKLG
     LEWIGFARWI VGARAVGSAE RLLQMAIDYS KERETFGRPI SDRQAIQWQI ADSAVEIEAA
     KWIVLNAAFT LDNGEDNRHL ASMAKLYGSN MGNRVVDRVM QIHGGMGYTK ELPIERWYRE
     ARLWRIYDGT DEIQRLIISR NLLKGNVKLG QYI
//
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