ID A0A0Q7D8H4_9CAUL Unreviewed; 394 AA.
AC A0A0Q7D8H4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQW71707.1};
GN ORFNames=ASC73_06335 {ECO:0000313|EMBL:KQW71707.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW71707.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW71707.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71707.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW71707.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71707.1,
RC ECO:0000313|Proteomes:UP000051150};
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:KQW71707.1}.
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DR EMBL; LMDZ01000004; KQW71707.1; -; Genomic_DNA.
DR RefSeq; WP_056019184.1; NZ_LMDZ01000004.1.
DR AlphaFoldDB; A0A0Q7D8H4; -.
DR Proteomes; UP000051150; 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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000051150}.
FT DOMAIN 6..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 394 AA; 43085 MW; E77B2934574421A6 CRC64;
MNLDLTAEEL GFRDEVRAFL EEALTPELRE AGRRATSVFM DKRYSLPWQK TLHARGWAAP
SWPKAYGGPG WSEMQRHIFA AECARAGAPS LAPMGLRMVG PVIMGYGTPE QKAHYLPRIL
SGEDYWCQGY SEPGAGSDLA SLQLRAVRDG DDYVLNGSKL WTTHAHWANR MFCLVRTLAD
GKPQAGITFL LLDMQSPGVR VRPIITLAGE HEVNEVFFED VRVPVSGRIG DENQGWTVAK
YLLEFERGGG SAPGLKVMLE RLRKAAREAG LLDEASFRGR LMETEIAVQA IEVSEQRILA
ALSSGKNPGP ASSMLKTQGG EAMQRIDELL LEVAGVYAAP DQPAAREPGS NTPPIGPDAL
LTAMPRYLND RAASIYGGSN EIQRDIIARL VLGL
//
