ID A0A1E8CUQ3_9MICO Unreviewed; 381 AA.
AC A0A1E8CUQ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OFE16055.1};
GN ORFNames=BA895_20815 {ECO:0000313|EMBL:OFE16055.1};
OS Humibacillus sp. DSM 29435.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Humibacillus.
OX NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE16055.1, ECO:0000313|Proteomes:UP000175826};
RN [1] {ECO:0000313|Proteomes:UP000175826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OFE16055.1}.
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DR EMBL; MAST01000019; OFE16055.1; -; Genomic_DNA.
DR RefSeq; WP_070192421.1; NZ_MAST01000019.1.
DR AlphaFoldDB; A0A1E8CUQ3; -.
DR STRING; 1869167.BA895_20815; -.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000175826; 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; COMPLEX I ASSEMBLY FACTOR ACAD9, 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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000175826}.
FT DOMAIN 8..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 381 AA; 42287 MW; CF3E920A1D79660C CRC64;
MPRHIYDEDH EALRASAREF VERTLRPRAQ QMIDEKSIER DVWKEAGKQG FFGFDIPEEF
GGAGVRDYRF NAVLSEEMSR FNAATSSCFG IHSDVCPPYI VDLGTDEQKQ RWLPGIASGD
LIIAIAMTEP SGGSDLAALK TTAVRDGDAW RLNGSKTFIT NGYQADLVIV AARTDPGKGA
KGITLFVVER GMPGFVNGRK LDKVGMEESD TAELFFEDVR VPDENRLGEQ GLGFIAMMQR
LPQERIGAAV SNVAHAKAIL EETIAYAKER KAFGQPIGSF QHNKFLLAEL VTKIEVAEAY
IDDCVLAHSK GELTAIDAAK AKWWSSQVQN EVLDHCVQLY GGYGFMNEYR VARAWRDARV
TKIWAGSNEI MKELIGRDIG L
//
