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Database: UniProt
Entry: A0A438M7S8_9ACTN
LinkDB: A0A438M7S8_9ACTN
Original site: A0A438M7S8_9ACTN 
ID   A0A438M7S8_9ACTN        Unreviewed;       384 AA.
AC   A0A438M7S8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:RVX41770.1};
GN   ORFNames=EDD27_4337 {ECO:0000313|EMBL:RVX41770.1};
OS   Nonomuraea polychroma.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX41770.1, ECO:0000313|Proteomes:UP000284824};
RN   [1] {ECO:0000313|EMBL:RVX41770.1, ECO:0000313|Proteomes:UP000284824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX41770.1,
RC   ECO:0000313|Proteomes:UP000284824};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JAN-2019) 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:RVX41770.1}.
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DR   EMBL; SAUN01000001; RVX41770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438M7S8; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000284824; 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   PIRSF; PIRSF016578; HsaA; 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.
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:UP000284824}.
FT   DOMAIN          5..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  41601 MW;  CDF09A50C17B5F62 CRC64;
     MSTLSEDERD IVALAGEFVD ERVRPRVRDY ESVDKYPAEF IEEMKKMGFF GLLAPAEHGG
     ADVSAACFAR VTEELARGWM SLAGAIGGHS VITYLIRAFG TPDQRERYLP PMADGTLRAT
     MALTEPGGGS DLQAMRTHAV ADGDDLLITG SKTWISNARH SGLIGLLCVT DQDARPAHQG
     MSVLLVEPGE GLHISKNLPK LGYRGVEACE LVFDRMRVPA SAVLGGAPNE GWAQMMRGLE
     VGRIQVAARA VGVAQAALDD AVTYAQERES FGKPIWKHQS VGNLLADMAT KVQAARLLTE
     DAARRLDEGV RADMEAGMAK LFASEAAMQV ALDAMRVHGG YGFSKEFEVE RYFRDAPLMI
     LGEGTNEIQR NVIAAQLIAR NPIN
//
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