ID A0A1H0PFH4_9ACTN Unreviewed; 384 AA.
AC A0A1H0PFH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SDP03520.1};
GN ORFNames=SAMN05660199_03069 {ECO:0000313|EMBL:SDP03520.1};
OS Klenkia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=1052260 {ECO:0000313|EMBL:SDP03520.1, ECO:0000313|Proteomes:UP000199088};
RN [1] {ECO:0000313|EMBL:SDP03520.1, ECO:0000313|Proteomes:UP000199088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45843 {ECO:0000313|EMBL:SDP03520.1,
RC ECO:0000313|Proteomes:UP000199088};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNIR01000009; SDP03520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0PFH4; -.
DR STRING; 1052260.SAMN05660199_03069; -.
DR OrthoDB; 3176804at2; -.
DR Proteomes; UP000199088; Unassembled WGS sequence.
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 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; 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; PTHR48083:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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.
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}.
FT DOMAIN 7..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..376
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 384 AA; 40629 MW; 2B0D4DB3CC162827 CRC64;
MEFAEKPELQ ALRETVGQIA ARYGSAYYVE RAAKHEPLTE LWADLAKAGF IGINVPEEYG
GGGGGLVELA IVCEEIAAQG CPMLLLLVSA AISAEVITRF GDDEQKQRWL PGLADGTSKV
VFAITEPGAG SNSHQLATSA RRDGDDWLIS GTKYYISGVD EAQALMVVAR TGTDEVSGKA
QMSLFLVPTD APGLVAQPLP VDAMLPERQF TLFFDDVRVG PEMVVGEVGA GFAQVFHGLN
PERITGAALC VGIARYALGK AAEYANQRTV WKAPIGAHQG VSHPLAKAAI ETELAALMTR
KAAWAHDSGV PAGEASNMAK YAAAEAALGA VDAAIQTHGG NGLSTEYGLV PYWGLARLLR
IAPVNREMVL NFVAQHTLGL PRSY
//