ID   A0A1I1IJ72_9RHOB        Unreviewed;       575 AA.
AC   A0A1I1IJ72;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05421762_0684 {ECO:0000313|EMBL:SFC36235.1};
OS   Pseudooceanicola nitratireducens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=517719 {ECO:0000313|EMBL:SFC36235.1, ECO:0000313|Proteomes:UP000231644};
RN   [1] {ECO:0000313|EMBL:SFC36235.1, ECO:0000313|Proteomes:UP000231644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29619 {ECO:0000313|EMBL:SFC36235.1,
RC   ECO:0000313|Proteomes:UP000231644};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOLX01000001; SFC36235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1IJ72; -.
DR   STRING; 517719.SAMN05421762_0684; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000231644; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231644}.
FT   DOMAIN          38..156
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          280..446
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          459..568
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   575 AA;  61385 MW;  9DD937AA40B927D3 CRC64;
     MPYRSPVSEY KFVLEHVVGF SDVSSTDTYA EATPDTVDAI LTEVAKLADE VMAPLNRNGD
     LDPARLENGV VRTSKGFADG YKAMTEGGWL GLAATPEYGG MGLPQTLSCA VNDFFAASCM
     SLGLNPLLTQ GHIEALEHHA PDWMKDLYLP KLISGEWSGT MNLTEPQAGS DVGALTSKAE
     PQGDGTYAIS GQKIYISWGD HDFGGNICHL VLARLPDAAP GTKGISLFMV PKYIPNEDGS
     LGEANSLRVV SLEHKLGIHG SPTCVMEYDR ATGWLVGEEN KGMAAMFTMM NNARLGVGIQ
     GIGIAEGAMQ HAIAYAMDRK QGRTPLDGTP EGTGTILDHA DVRRMVATMK ADTFAARAIA
     LACGVGIDMT AATGDKAWTA RAAFLTPIAK AFGTEVGMRV SELGVQIHGG MGFIEETGAA
     QYSRDVRVTA IYEGTNGIQA MDMVARKMMD GGETANAIID EIEATAEEAR AKLPDLGEAV
     WQSAETLREA TEWMTAQGEL NERFAGAVPY LMGFARVLGA HYHLKAALAE GDNGPRTRLA
     RFYITRLLPE HIGHLAHATC GAEDLYALTT DELTA
//