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Database: UniProt
Entry: A0A2N0ETK9_9FLAO
LinkDB: A0A2N0ETK9_9FLAO
Original site: A0A2N0ETK9_9FLAO 
ID   A0A2N0ETK9_9FLAO        Unreviewed;       380 AA.
AC   A0A2N0ETK9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATE92_1562 {ECO:0000313|EMBL:PKA83410.1};
OS   Ulvibacter sp. MAR_2010_11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=1250229 {ECO:0000313|EMBL:PKA83410.1, ECO:0000313|Proteomes:UP000232889};
RN   [1] {ECO:0000313|EMBL:PKA83410.1, ECO:0000313|Proteomes:UP000232889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_11 {ECO:0000313|EMBL:PKA83410.1,
RC   ECO:0000313|Proteomes:UP000232889};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (NOV-2017) 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:PKA83410.1}.
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DR   EMBL; PHTY01000001; PKA83410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0ETK9; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000232889; 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; 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; 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}.
FT   DOMAIN          6..118
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          231..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41538 MW;  699F2CA91C187C18 CRC64;
     MDFNLSEEHL MIRDAARDFA RTELLPGVIE RDNLQKFPTE QVKKMGELGF LGMMVDPKYG
     GGGMDTVSYV LAMEELSKID ASSSVVVSVN NSLVCYGLQA FGSEEQKQKY LTKLATGQSI
     GAFCLSEPEA GSDATSQRTT AIDMGDHYIL NGTKNWITNG GTADYYLVIA QTDKEKGHKG
     INALIVEKGW AGFEIGPKED KLGIRGSDTH SLIFNDVKVP KENRIGDDGF GFKFAMKTLS
     GGRIGIAAQA LGIAAGAYDL AREYSKVRKS FGTEICNHQA IAFKLADMHT SITAARHLVM
     KAAWDKDQGN NYDMSGAMAK LYASQVAMDV TVEAVQVHGG NGYVKEYHVE RLMRDAKITQ
     IYEGTSEIQK IVISRGLLRD
//
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