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Database: UniProt
Entry: A0A3D8L9J9_9BACT
LinkDB: A0A3D8L9J9_9BACT
Original site: A0A3D8L9J9_9BACT 
ID   A0A3D8L9J9_9BACT        Unreviewed;       599 AA.
AC   A0A3D8L9J9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RDV14091.1};
GN   ORFNames=DXT99_16110 {ECO:0000313|EMBL:RDV14091.1};
OS   Pontibacter diazotrophicus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV14091.1, ECO:0000313|Proteomes:UP000256708};
RN   [1] {ECO:0000313|Proteomes:UP000256708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA   Liu Z.-W., Du Z.-J.;
RL   Submitted (AUG-2018) 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:RDV14091.1}.
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DR   EMBL; QRGR01000018; RDV14091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8L9J9; -.
DR   OrthoDB; 9764422at2; -.
DR   Proteomes; UP000256708; 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:UP000256708}.
FT   DOMAIN          34..146
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          150..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          255..417
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..571
FT                   /note="Acyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21263"
SQ   SEQUENCE   599 AA;  66353 MW;  126A88E05BC13A46 CRC64;
     MANTTENKTA VLQGGEFLIK ETNPQDVFIP AEFNEEQQMM AQTCRDFVRE EVWPLLERLD
     NHEEGLMENL MKKAGELGLF AVSIPEQYGG LNMDFNTALL VTESVGGGHS FPVAFAAHTG
     IGMLPILYFG TEEQKQNYIP KLVSGEWTSA YCLTEPGSGS DALAAKTKAV LNEAGTHYIL
     NGQKMWITNA GFADVFVVFA QIDGDKFTGF IVERGYKGVS LGNEEHKMGI KGSSTRQVFF
     EDCEVPKENV LGEIGKGHLI AFNILNIGRI KLCAATLGAS KHVADLSVKY ANERHQFKLP
     ISKFGAIKYK LAEQAIRIYA VESALYRCGM DIYRKEQELM AGGADENEAL LGAAREFAVE
     CAMLKVEGSE VLDYVVDEGV QIYGGYGFSA DYPMDRAYRD SRINRIFEGT NEINRMLTVD
     MILKKAMKGE LDLMGPAQAV QQELMAIPDF GAEEEEGLFT AEHKAIRNLK KAILLTAGTA
     VQKYMNSLAK EQEVLMNIAD MAIKTYVAES TLLRVEKLVS QKGEEAAANE MDIVRVVVND
     AVDTTFRAGK EAIAAMAEGD EQRLLFMGLK RFTKRDLYNT KEARRRIAAA MIEANEFVY
//
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