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Database: UniProt
Entry: A0A0Q7AW26_9BURK
LinkDB: A0A0Q7AW26_9BURK
Original site: A0A0Q7AW26_9BURK 
ID   A0A0Q7AW26_9BURK        Unreviewed;       409 AA.
AC   A0A0Q7AW26;
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:KQW40116.1};
GN   ORFNames=ASC76_01285 {ECO:0000313|EMBL:KQW40116.1};
OS   Rhizobacter sp. Root404.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW40116.1, ECO:0000313|Proteomes:UP000051611};
RN   [1] {ECO:0000313|EMBL:KQW40116.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW40116.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW40116.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW40116.1,
RC   ECO:0000313|Proteomes:UP000051611};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:KQW40116.1}.
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DR   EMBL; LMDS01000001; KQW40116.1; -; Genomic_DNA.
DR   RefSeq; WP_056461236.1; NZ_LMDS01000001.1.
DR   AlphaFoldDB; A0A0Q7AW26; -.
DR   STRING; 1736528.ASC76_01285; -.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000051611; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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   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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT   DOMAIN          11..136
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          140..242
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          254..404
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   409 AA;  46087 MW;  B49B42D747D79F31 CRC64;
     MEFEFSPKVV ELRERLLKFM DDHVYPNEQR REEELAANAK AGRPYAELPM MAGLKAKARE
     QGLWNLFLPP HPGDTHAPTG LTNVEYAPLC EIMGRRYWCA EIFNCSAPDT GNMEVLARYG
     TPAQQARWLT PLLAGEIRSS FAMTEPEVAS SDATNIQCSI RREGDEYVIN GRKWYITGAM
     NERCEIFVLM GKTDPDHADR HKQQSMILVP KDTPGITIVR DMALLGVYDP PFGHPEIVFE
     NVRVPVSNIL LGEGRGFEIA QGRLGPGRIH HCMRAIGMAE AALEMMCRRL ASRTAFRKLL
     ADQGVWRERI AESRMLIDQS RWMVLNAAHR MDTVGNKVAA KEIAMIKVLT PNNCVKVIDW
     AMQAFGAMGL SQDTLLTSFY AYERHLRVAD GPDEVHRNAI AKQELAAYL
//
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