ID Q6A5P3_CUTAK Unreviewed; 382 AA.
AC Q6A5P3;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AAT83920.1};
GN OrderedLocusNames=PPA2216 {ECO:0000313|EMBL:AAT83920.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT83920.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT83920.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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}.
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DR EMBL; AE017283; AAT83920.1; -; Genomic_DNA.
DR RefSeq; WP_002514161.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A5P3; -.
DR EnsemblBacteria; AAT83920; AAT83920; PPA2216.
DR KEGG; pac:PPA2216; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_11; -.
DR Proteomes; UP000000603; Chromosome.
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; 2.
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}.
FT DOMAIN 6..117
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 228..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 382 AA; 41283 MW; C5744FF667198CB7 CRC64;
MLYHLSEEHE MLRQFVREFA ESQLAPNAAE VDDKGVFAQQ QYDALVEAGF AAPGIPEQYG
GDGADAIASA IIMEEVARVC ASSSTVISSN ELGTVPLLKY GSEEQRKRYL SEVASGKALF
GYALSEADAG SDPAALKCRA DEDGDSFVLN GVKAWVTEAG EAKYLVVFAV TDPDDPRHRI
SALMVHADDP GISYGAPEHK MGIRGSVTRE VVFKNTRIPK ERVIGRRGHG LSVALGTLDN
SRVSIAAQAV GIAQGALDIA TDYVQKRKQF GQPLSNFEGI QFMLADMAMR LEAARALTYS
AADRSGRQTD DVSYFGAAAK CFASDTAMAV CTDAVQLLGG IGYSKDSAVE RMFRDAKVTQ
IYEGTNQIQR IVIARQLFNR SR
//
