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Database: UniProt
Entry: A0A0B2AL56_9MICC
LinkDB: A0A0B2AL56_9MICC
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ID   A0A0B2AL56_9MICC        Unreviewed;       395 AA.
AC   A0A0B2AL56;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KHL04041.1};
GN   ORFNames=LK10_07315 {ECO:0000313|EMBL:KHL04041.1};
OS   Sinomonas humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL04041.1, ECO:0000313|Proteomes:UP000030982};
RN   [1] {ECO:0000313|EMBL:KHL04041.1, ECO:0000313|Proteomes:UP000030982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL04041.1,
RC   ECO:0000313|Proteomes:UP000030982};
RA   Lee L.-H.;
RT   "Genome sequence of Sinomonas sp. MUSC 117.";
RL   Submitted (SEP-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:KHL04041.1}.
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DR   EMBL; JTDL01000087; KHL04041.1; -; Genomic_DNA.
DR   RefSeq; WP_043121717.1; NZ_JTDL01000087.1.
DR   AlphaFoldDB; A0A0B2AL56; -.
DR   STRING; 1338436.LK10_07315; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000030982; 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   CDD; cd00567; ACAD; 1.
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   PIRSF; PIRSF016578; HsaA; 2.
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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030982}.
FT   DOMAIN          11..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..210
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          223..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   395 AA;  43682 MW;  EDD41653A1652E07 CRC64;
     MEFGYTPRLV ELKQRARDLT TKMMQFEDEC EANNGLSAES HAVIKEAVLS AGLQAINTPT
     EFGGAGLTVL EQVVVQDELG KLTNALWDAV WRPANPLAHA TEEQRARYLI PEARGERRDA
     VAITEADAGS DPTGIQTTAH RDGEGFVING EKWFVTVGDV ADFLLVLANV PDEGPTMFLV
     DVDQPGVTVA KVPRYTHTFV YEHPEFHFTN VRVGADAVLG GVGNGYELTR DWFTEERLMI
     GARTIGAAER ALDLAIEWAK QREQGGEKLI DRQLIQGMIA DSVADIATNR ALTHQVAWEF
     DNSDLSDPNV RKTLHAKAAT VKLAASEASN RVVDRAQQIF GGRGYMRDYA VERLWRELRV
     DRIWEGTSEI QRLVIANETK KRGLAGLVSF RGPEA
//
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