ID B9CZ00_CAMRE Unreviewed; 378 AA.
AC B9CZ00;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000313|EMBL:EEF15017.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:EEF15017.1};
GN ORFNames=CAMRE0001_1573 {ECO:0000313|EMBL:EEF15017.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF15017.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF15017.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF15017.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) 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:EEF15017.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACFU01000003; EEF15017.1; -; Genomic_DNA.
DR AlphaFoldDB; B9CZ00; -.
DR STRING; 553218.CAMRE0001_1573; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000003082; 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 CDD; cd00567; ACAD; 1.
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; 2.
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.
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 7..108
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 226..374
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 378 AA; 42792 MW; 059DB3EA1B808568 CRC64;
MMDFKLTDEQ ELFVAGVREL MERENWEAYF AKCDEAHEYP IKWVKELAEL GVDTMLLPEE
HGGMDASWVT LAAIWEELGR CGAPTYVLYQ LPGFSTILKY GSQEQIDKIF AFRGTGKQMW
NSAITEPGAG SDVGSLKTTY TKKDGKVYLN GQKCFITSSA HTPYIVVMAR DSQSEKPIFT
EWFVDMSKPG IKLTPLDKLG LRMDSCCEIV FDNVELEEKD VFGEYGNGFN RVKEEFDAER
FLVACTNYGI AYCAFEDAAK YANQRVQFGE TIGRTQLIQE KFAHMAMRLN AMKYMVYSTA
WKMDQGLNVT GESAMCKFYC ANNAFAVVDD AIQVLGGIGV TGHRVSRFWR DLRVDRLSGG
SDEMQILTLG RAILKQYR
//
