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Database: UniProt
Entry: A0A098Y893_9ACTN
LinkDB: A0A098Y893_9ACTN
Original site: A0A098Y893_9ACTN 
ID   A0A098Y893_9ACTN        Unreviewed;       387 AA.
AC   A0A098Y893;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGH46667.1};
GN   ORFNames=IN07_11010 {ECO:0000313|EMBL:KGH46667.1};
OS   Modestobacter caceresii.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH46667.1, ECO:0000313|Proteomes:UP000029713};
RN   [1] {ECO:0000313|EMBL:KGH46667.1, ECO:0000313|Proteomes:UP000029713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH46667.1,
RC   ECO:0000313|Proteomes:UP000029713};
RA   Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT   "Biosystematic studies on Modestobacter strains isolated from extreme
RT   hyper-arid desert soil and from historic building.";
RL   Submitted (JUL-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:KGH46667.1}.
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DR   EMBL; JPMX01000043; KGH46667.1; -; Genomic_DNA.
DR   RefSeq; WP_036335774.1; NZ_JPMX01000043.1.
DR   AlphaFoldDB; A0A098Y893; -.
DR   STRING; 1522368.IN07_11010; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000029713; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
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:UP000029713}.
FT   DOMAIN          16..128
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..229
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          272..384
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   387 AA;  41497 MW;  2CD081F5085C2881 CRC64;
     MGSNSLTLAP APRSAAAEEV RAEVREFLAA ELAAGSFTTH VDTWLSGVDP AFSRKLGERG
     WLGMTWPKQY GGHERTAMER YAVTEELLAA GAPVAAHWIA DRQSGPNLLR YGTEAQRAEI
     LPRIAAGECY FVIGMSEPDS GSDLASIRTR ATRNGDGDWV VNGAKVWTSN AHTSHYAITL
     VRTSPADPAS RHAGLSQLLV DLSLPGITVN PIRILDGGHH FNEVVFEDVV IPGDMLLGEE
     GAGWHQVTAE LAFERSGPER FLSTYPLIAE FARRAAEGQD PAQLATLGRL SARLLALRQL
     SLRIAGALDR GELPDIPAAL VKDVGTTFEA DVIDEVRRVV DVPASLDSPD PLGRALAEAQ
     LHAPGYTLRG GTNEILRGIV ARGLGLR
//
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