ID A0A2S5X7Z2_9MICO Unreviewed; 392 AA.
AC A0A2S5X7Z2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PPG40866.1};
GN ORFNames=C5C17_08270 {ECO:0000313|EMBL:PPG40866.1};
OS Pseudoclavibacter sp. RFBA6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pseudoclavibacter.
OX NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG40866.1, ECO:0000313|Proteomes:UP000237697};
RN [1] {ECO:0000313|EMBL:PPG40866.1, ECO:0000313|Proteomes:UP000237697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RFBA6 {ECO:0000313|EMBL:PPG40866.1,
RC ECO:0000313|Proteomes:UP000237697};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:PPG40866.1}.
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DR EMBL; PSUA01000010; PPG40866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5X7Z2; -.
DR Proteomes; UP000237697; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000237697}.
FT DOMAIN 16..90
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 242..362
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 392 AA; 42251 MW; 92B009F0CD389761 CRC64;
MPASDPRSIL ADELLEVLNQ RASRYDAENS FPTDDLEALR EDGYLRLLVP RDFGGTGATL
EQAVRCQARL AAAAPATALA VNMHHVVAGI ARARHESDDD GLDWMLREIV AGETYALAIS
EIGNDAVLYD SNVRAEPEQG GGYRLHGMKI FTSLSPVWTR LVTFGRDDTG AEPALVHGVL
RRNDDGVRIH DDWDTLGMRA TQSCSTSLDG ALIPADRVIA RLPVGPNGEP HIFAVHSNFL
LLVAACYVGI GDRALELAVD AAKHRSSSTQ GGMRLADDVQ VREEIARMSI RQLAARTLVE
SIARDVDEGA PHGDTWFARL TMAKYEAVAA AAATTHDALG IVGGSGYRSG HELARLLRDV
LAGGLHPSNE RAVRRLHAGH RLGPIQDPPT SH
//
