ID A0A0Q4GI12_9SPHI Unreviewed; 453 AA.
AC A0A0Q4GI12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQM77278.1};
GN ORFNames=ASE74_18725 {ECO:0000313|EMBL:KQM77278.1};
OS Pedobacter sp. Leaf216.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM77278.1, ECO:0000313|Proteomes:UP000051744};
RN [1] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Garrido-Oter R., Mueller D.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQM77278.1}.
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DR EMBL; LMKM01000007; KQM77278.1; -; Genomic_DNA.
DR RefSeq; WP_055906416.1; NZ_LMKM01000007.1.
DR AlphaFoldDB; A0A0Q4GI12; -.
DR STRING; 1735684.ASE74_18725; -.
DR OrthoDB; 1522475at2; -.
DR Proteomes; UP000051744; 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 GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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; 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|RuleBase:RU362125}.
FT DOMAIN 80..186
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 194..287
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 304..446
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 453 AA; 50342 MW; 39A6313D6025C663 CRC64;
MANIFSSLKN AYNLFKHVDF DKLEALSKKV DLPKMVETIS SLDDKQIQGM MKMMGGSGKK
RELPPIEGDF YHLGDEALKE EDRELQLKVR AFLEKEVKPI VNHYWNKAEF PFEIIPKLAE
LNICGLTYKG YGCPGKSNLM EGILAMEMAR IDTSISTFFG VQSGLAMGSI YLCGSEEQKQ
QWLPLMQQFK IIGAFGLTEP EVGSAAAGGL TTTCKKVDGK WVLNGQKKWI GNATFADILI
IWARDEDSGE VKGFIVKKDN PGFAVEKMQD KMALRIVQNG IITLTNCEVD EADRLQNANS
FKDTAKVLQM TRAGVAWQAV GCARGAYENA LAYTRTRKQF GKPIASFQLI QNHLVEMLSN
LTAMQTLCFR LSQLQDQGLL KDEHASLAKV FCSLRTRDVV SKAREVMGGN GILLEYNVAR
FVADAEAIYS YEGTKEINTL IVGRAITGFS AFV
//
