ID A0A0Q7TDH7_9CAUL Unreviewed; 407 AA.
AC A0A0Q7TDH7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQY92729.1};
GN ORFNames=ASD21_15265 {ECO:0000313|EMBL:KQY92729.1};
OS Caulobacter sp. Root1455.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736465 {ECO:0000313|EMBL:KQY92729.1, ECO:0000313|Proteomes:UP000051447};
RN [1] {ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|Proteomes:UP000051447};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY92729.1, ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|EMBL:KQY92729.1,
RC ECO:0000313|Proteomes:UP000051447};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQY92729.1}.
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DR EMBL; LMFQ01000024; KQY92729.1; -; Genomic_DNA.
DR RefSeq; WP_056445830.1; NZ_LMFQ01000024.1.
DR AlphaFoldDB; A0A0Q7TDH7; -.
DR Proteomes; UP000051447; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
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|RuleBase:RU362125}.
FT DOMAIN 6..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..386
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 407 AA; 43853 MW; 98E33164A4384133 CRC64;
MDFNDSPEEA AYREKARAWL VEAAAAHRAE HGEPKPTTPE HMAAGKAWQA RKAAAGYACI
TWPAGVGGGG GTPIQSVIFG QEEAKAGVGY GYFTIGLGMC VPTVMAFADD ATKQRFVSPA
VKGEEIWCQL FSEPAGGSDV AALRTRAVKD GDDWVINGQK VWTTGAHYCD YGILLVRTDP
DVPKHKGLTM FWIDMRDPAV ECRPIHQMSG GREFNEVYFT DLRVKDSQRL GAVGDGWKVA
LVTLMNERLA VGGSAGPDYR QVMELARGLS GANGPALKDA AFREKLADWY VNSQGLKFTR
FRTMTALSRG QTPGPESSIG KIISANQLQD LANTAVEAQG EYGILTDPAL APMEAAFQAS
LMWAPGLRIA GGTDEILKNI IAERVLGLPG DVRVDKDVAF KDMPTGR
//
