ID A0A1N7N568_9RHOB Unreviewed; 560 AA.
AC A0A1N7N568;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN05421580_10737 {ECO:0000313|EMBL:SIS93485.1};
OS Rhodobacter aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=453582 {ECO:0000313|EMBL:SIS93485.1, ECO:0000313|Proteomes:UP000186221};
RN [1] {ECO:0000313|Proteomes:UP000186221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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}.
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DR EMBL; FTOG01000007; SIS93485.1; -; Genomic_DNA.
DR RefSeq; WP_076485090.1; NZ_QAXT01000002.1.
DR AlphaFoldDB; A0A1N7N568; -.
DR STRING; 453582.SAMN05421580_10737; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000186221; 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:UP000186221}.
FT DOMAIN 78..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..432
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 448..553
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 560 AA; 59437 MW; 41B3619754739E52 CRC64;
MAYRSPVADI RFILDKVVPL APVAATERFA EATGDTVEAV LLEAGKLCDE VMAPLLRAGD
LHPAKLENGV MRTSPGFKDA YAQIAEGHWV AVAASHEFGG MGLPQTLCVA INDMMSGANL
ALQLKPLLTQ GQIEALEHHA SDTLKALYLP KLISGEWSGT MNLTEPQAGS DVGALRSKAE
PLGDGTYAIT GQKIFISWGD SDMVENVCHL VLARLPDAVP GTKGISLFMV PKFLPDAAGN
PGTANSLKVV SLEHKMGLHG SPTCVMSFEG ATGWLVGEPG KGMAAMFTMM NNARLAVGVQ
GIGVAEGAYQ KALAYAQERV QFAPIIEHAD VRRMLAEMRA DIFAARSIAL ACAVALDMGR
ATGEADWHAR AALLTPIAKA YGTDVGIHVA DQGIQVHGGM GFVEETGAAQ YLRDVRVTAI
YEGTNGIQAM DLVGRKMMDD GRAAFRLLQE VEDAAKAARE TLPDLAEAVW QAAETMREAT
EGLIAQGTQD RFAGAVPYLR AFARVLGAHY HLKAALADEV RAKLAAVYIR RILPQTEADL
ASVRAGAVDL YALSPEDLGA
//
