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
//