ID A0A133XNC0_9RHOO Unreviewed; 593 AA.
AC A0A133XNC0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KXB32431.1};
GN ORFNames=AT959_01720 {ECO:0000313|EMBL:KXB32431.1};
OS Dechloromonas denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB32431.1, ECO:0000313|Proteomes:UP000070186};
RN [1] {ECO:0000313|EMBL:KXB32431.1, ECO:0000313|Proteomes:UP000070186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB32431.1,
RC ECO:0000313|Proteomes:UP000070186};
RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT versus atypical NosZ.";
RL Submitted (DEC-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:KXB32431.1}.
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DR EMBL; LODL01000005; KXB32431.1; -; Genomic_DNA.
DR RefSeq; WP_066879952.1; NZ_LODL01000005.1.
DR AlphaFoldDB; A0A133XNC0; -.
DR STRING; 281362.AT959_01720; -.
DR Proteomes; UP000070186; 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; IPR020953; Acyl-CoA_DH_N_bac.
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 Pfam; PF12418; AcylCoA_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:UP000070186}.
FT DOMAIN 4..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 40..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 467..588
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 593 AA; 62827 MW; F3139B32AF6364E5 CRC64;
MSEYIAPLKD IRFAMQELAG LEQVVALPGC EEASPDVVDA ILEEAARFSA EVLSPLNAVG
DKNGAKWKDT VVTTTPGFKE AYRQFVDNGW NGLGCDPEFG GQGLPRLLSA AVSEMWKASN
HAFSLCPMLT QGAIEALMIA GTDAQKAAYL PNLVSGEWTG TMNLTEPSAG SDLAAVRSRA
EPVGDGSYRI FGQKIFITYG EHDMTDNIVH LVLARTPNAP EGVKGISLFV VPKFMLKADG
TPGERNDVYC VSIEHKLGIH GSPTAVLAFG DNGGAIGTLV GEENRGLEYM FIMMNAARFN
VGLEGLGDAE RAYQRAVVYA RERVQGAEVG VRGGPKVPII KHPDVRRMLM SMRARIEAMR
ALAYVTAAAQ DHAHGNLDQV ARQRGQAFAD LMIPVIKGWS TESAIDIASI GVQVHGGMGY
IEETGAAQHL RDARITSIYE GTTAIQANDL IGRKIAREQG ATIRSVIAEM RAAATALDGD
LAGVGARQSA AVDALEKAVS WIVDNFAADP KAAHAGAVPF LYLLGIVAGG WQMGRAAVIA
RARLAAGDAD PFWAAKLATT RFYADHFLTQ AAGLAEAVTT GAAGALAIAD DSF
//
