ID L7LP53_9ACTN Unreviewed; 368 AA.
AC L7LP53;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAC62915.1};
GN Name=fadE {ECO:0000313|EMBL:GAC62915.1};
GN ORFNames=GSI01S_50_00040 {ECO:0000313|EMBL:GAC62915.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC62915.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC62915.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC62915.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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:GAC62915.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BANU01000050; GAC62915.1; -; Genomic_DNA.
DR AlphaFoldDB; L7LP53; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000035083; 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 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035083}.
FT DOMAIN 1..107
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 111..208
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 220..368
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 368 AA; 40065 MW; CCA0F93984218735 CRC64;
MLRDHARAFF AREVTPRQAD WARQGHVDRE LWNRAGAAGL LLTDIAEKDG GGGGDFGHEA
VVAQELAYAH DSAFGFTVHS TIVSHYINAY GTEEQKRRWL PGLASGEKVV AVAMTEPGTG
SDLQNVKTTA IRDGDHYVVN GAKTFISNGT HCDLVVIVAK TDPAAGGKGI SLLVAEVDNN
VAGFSRGAVL EKIGMHGWDT RELFFDDMRV PVENILGEEG SGFAELMTQL PRERLIIGVA
GVAVAEAAVI ETIRYVKERD AFGKKLLDFQ NTQFVLAECK ADVYAGKALI DDGIRRQIDG
TLDAAGASMI KLWATDMQCR VVDKCLQLFG GYGYMMEYPI AQMYTASRVQ RIYGGTNEIM
KLLVARSL
//
