ID A0A0N8W581_9SPHI Unreviewed; 593 AA.
AC A0A0N8W581;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQB99962.1};
GN ORFNames=AQF98_15765 {ECO:0000313|EMBL:KQB99962.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB99962.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQB99962.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQB99962.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) 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:KQB99962.1}.
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; LLWP01000008; KQB99962.1; -; Genomic_DNA.
DR RefSeq; WP_055132912.1; NZ_LLWP01000008.1.
DR AlphaFoldDB; A0A0N8W581; -.
DR STRING; 1740090.AQF98_15765; -.
DR OrthoDB; 1522475at2; -.
DR Proteomes; UP000050543; 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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_C; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT DOMAIN 29..140
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 145..238
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..412
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 462..565
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 593 AA; 65275 MW; C2B3F8E7849A5307 CRC64;
MEKKTIKGGE FLITETTYQD VFIPEEFDEE QQMIAQTCRD FLAAEVNPIL DRIDSQEEGL
MPSLMDKAGE LGILGVSIPE EFGGFGKNFN TSMLVADVCG AGHSFAVALS AHTGIGTLPI
LYYGNAEQKA KYIPKLGTGE WKASYCLTEP NSGSDANSGK TKAKLSADGK HYIINGQKMW
ITNGGFADIF IVFAKIDDDK NLTAFIVEKD FGGITMNPEE HKMGIKGSST RQVFFNDCPV
PVENMLSERE NGFKIAVNIL NIGRIKLAAA AIGGSKGVLN LAVNYSNERI QFDRPISKYG
AIRYKIAEMA AKVYAVESAN YRAGQNIDDA YDELVAAGMD AGKAKLKSTE QFAVECAILK
VWGSEVLDYV TDEGVQIYGG MGFSADAPMD RSYRDARINR IFEGTNEINR LLTVDMMLKR
AMKGELDLMT PATAVAAELM SIPDFGEEDT TLFAAEKKVI QNLKKATLMV AGAAVQKLMM
SLSKEQEILM NIADMASYVY IAESAMLRTE KLVALRGEEA CKGQLDMMRI YFVEAVDGLA
KAGKEALWAF AEGDEQRMML VGLRRFTKME PFNVKQARQN VAQQIIEANK YIF
//
