ID A0A317MPE2_9ACTN Unreviewed; 375 AA.
AC A0A317MPE2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:PWV58095.1};
GN ORFNames=BDW27_101332 {ECO:0000313|EMBL:PWV58095.1};
OS Nocardiopsis sp. L17-MgMaSL7.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1938893 {ECO:0000313|EMBL:PWV58095.1, ECO:0000313|Proteomes:UP000246681};
RN [1] {ECO:0000313|EMBL:PWV58095.1, ECO:0000313|Proteomes:UP000246681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L17-MgMaSL7 {ECO:0000313|EMBL:PWV58095.1,
RC ECO:0000313|Proteomes:UP000246681};
RA Partida-Martinez L.;
RT "The Agave Microbiome: Exploring the role of microbial communities in plant
RT adaptations to desert environments.";
RL Submitted (MAY-2018) 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|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:PWV58095.1}.
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DR EMBL; QGTF01000001; PWV58095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MPE2; -.
DR Proteomes; UP000246681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; 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:SF25; ACYL-COA DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 240..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 269..338
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 375 AA; 39814 MW; 8975415D98F21FA5 CRC64;
MIVHRDRAAL EALLPGLDAE LTKRSLSDLE STENDGLSLY RRFGGCGLLI PKENGGLAAD
AHTAIRAIRA LAGRSPSLAV AATMHNFSVA SLVALATHSN GFEWMLLDAV ASDRLLVCSA
FAEGRSGQGV LAPTMRARRE NDHWVIDGRK KPCSLSRSMN LITASVALED ADGGEPQFGV
ALIPAETPGI SVRPFWNSQV LTGAESDELI LDNVIVGDDL VVRPELDPGS NLDNLQTTGM
IWFSLLIAGG YLGMAGALVE RLWDSGRDRD RCATALLELE AADLALASVA SELDSGAADN
GVLARALTAR YAAHDTSRRV ADSCVEALGG MGFVSSRDVS YLVSATHAGQ FHPPSRRSAL
TSFHDYFDGS ALRID
//
