ID A0A2T7UWA4_9RHOB Unreviewed; 423 AA.
AC A0A2T7UWA4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PVE48849.1};
GN ORFNames=DDE23_00115 {ECO:0000313|EMBL:PVE48849.1};
OS Pararhodobacter aggregans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE48849.1, ECO:0000313|Proteomes:UP000244810};
RN [1] {ECO:0000313|EMBL:PVE48849.1, ECO:0000313|Proteomes:UP000244810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-19 {ECO:0000313|EMBL:PVE48849.1,
RC ECO:0000313|Proteomes:UP000244810};
RX PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA Foesel B.U., Drake H.L., Schramm A.;
RT "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT biofilter of a marine aquaculture.";
RL Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE48849.1}.
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DR EMBL; QDDR01000001; PVE48849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7UWA4; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000244810; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000244810}.
FT DOMAIN 15..128
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 132..234
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 246..394
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46969 MW; 31C6094E549FB0D6 CRC64;
MVPDKSPRVL DYEARLKAFM DEHIYPNEAE FFREAEELGP FAIYPMFDRL KPKAREAGLW
NLFLPDSDKG AGLSNVEYGY LCEIMGRSFL APEVFNCNAP DTGNMEVIER YGSAEHKERW
LKPLLNGEIR SCFAMTEPAV ASSDATNIQA EIRREGDNYV INAHKWYTTG ASNPKTKICI
FMGKTDPGNP DRHKQQSMIL VPMDTPGITV TRSLPVFGYY GVPDRASEVL FQDVRVPASN
LLLGEGRGFE IAQGRLGPGR IHHCMRTIGM AERLLEIMID RTLQRVAFGK PVAEQGVTRE
RIAEARLMID QCRLLTLHAA HKMDTVGNKE ARAEIAMIKI AAPTMACQIA DWAIQACGGG
GTGNDFGTAL AYAGLRTLRL ADGPDEVHRD QLARMEIKKR RGLNHPGWAP QVTNRGRNPA
LGG
//
