ID A0A1B3ZG33_9SPHN Unreviewed; 395 AA.
AC A0A1B3ZG33;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AOH86388.1};
GN ORFNames=AWL63_00490 {ECO:0000313|EMBL:AOH86388.1};
OS Sphingomonas panacis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH86388.1, ECO:0000313|Proteomes:UP000094256};
RN [1] {ECO:0000313|EMBL:AOH86388.1, ECO:0000313|Proteomes:UP000094256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY99 {ECO:0000313|EMBL:AOH86388.1,
RC ECO:0000313|Proteomes:UP000094256};
RA Kim Y.J., Yang D.C., Sing P.;
RT "Complete genome and mega plasmid sequence of Sphingomonas panacis DCY99
RT elicits systemic resistance in rice to Xanthomonas oryzae.";
RL Submitted (JAN-2016) 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}.
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DR EMBL; CP014168; AOH86388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B3ZG33; -.
DR STRING; 1560345.AWL63_00490; -.
DR KEGG; span:AWL63_00490; -.
DR Proteomes; UP000094256; Chromosome.
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; 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 15..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 120..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 395 AA; 44210 MW; CBF48C4B0C149C0B CRC64;
MDEHIVPAVP IYQQQLAAID RWAEIPPIFE QLKAKARAEG LWNIFMPPSE HDDAFFTSVG
LTNVEYAPIA ELMGRVSFAS EVFNCMAPDT GNFEVLHRYG TPAQKQRFMV PLRDGETRSA
FLMTEPAVAS SDARNIQTEI RREGDEYVVN GRKWWSSGAG HPHCAFYIVM GKTDPNAAPY
HQQSMILVPR NTPGITLVRH LPVFGYDHAP HGHFEVLLEN VRVPAENMLL GEGRGFEIAQ
GRLGPGRIHH TMRNIATMEV ALEKTCRRLL SRRAFGKAIA EHSVWEERIA RARCEIEMAR
LLCLKAAHMM DTVGNKEARA EIAMIKIAAP KMAQQIVDDA IQAHGGGGVS DDFGLAELWA
NTRIVRLTDG PDEVHERQLA RMELAKYRER DGATS
//
