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Database: UniProt
Entry: A0A0Q6RRY2_9MICO
LinkDB: A0A0Q6RRY2_9MICO
Original site: A0A0Q6RRY2_9MICO 
ID   A0A0Q6RRY2_9MICO        Unreviewed;       384 AA.
AC   A0A0Q6RRY2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQV26813.1};
GN   ORFNames=ASC54_03635 {ECO:0000313|EMBL:KQV26813.1};
OS   Yonghaparkia sp. Root332.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microcella.
OX   NCBI_TaxID=1736516 {ECO:0000313|EMBL:KQV26813.1, ECO:0000313|Proteomes:UP000051768};
RN   [1] {ECO:0000313|EMBL:KQV26813.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV26813.1,
RC   ECO:0000313|Proteomes:UP000051768};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV26813.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV26813.1,
RC   ECO:0000313|Proteomes:UP000051768};
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:KQV26813.1}.
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DR   EMBL; LMCX01000001; KQV26813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6RRY2; -.
DR   STRING; 1736516.ASC54_03635; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000051768; 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   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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051768}.
FT   DOMAIN          9..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  41202 MW;  F3C2302C84B2E3BC CRC64;
     MAAPAHGLSD EQQALVEMVR DFAQQELEPH AIEWDREKHF PLDVLHAAGE LGFGGIYVRE
     DVGGTELTRA DTALIFEELA KGDVTIAAYI SIHNMVAWMI DTFGDDDQRE RWVPRLASME
     HLGSYCLTEP DSGSDAGALA TRAVRDGDDY ILTGVKQFIS GAGSTDVYIV MARTGEAGPG
     GITAFIVPAD APGLSFGPNE VKMGWNAQPT RPVILDGVRV PAADRLGAEG EGFTMAMKAL
     NGGRLNIAAC SLGGAQWALD RAVRHISTRR AFGAPLSTQQ SLVFTIADME TELQAARLLL
     RSAAQSIDSG HPDVAAHCAM AKRFATDVAF TAANAALQLH GGYGYLAEYG IEKVVRDLRV
     HQILEGTNEI MKLIIGRSVL EKVS
//
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