ID S5YID4_PARAH Unreviewed; 375 AA.
AC S5YID4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AGT11238.1};
DE EC=1.3.8.- {ECO:0000313|EMBL:AGT11238.1};
GN ORFNames=JCM7686_pAMI5p172 {ECO:0000313|EMBL:AGT11238.1};
OS Paracoccus aminophilus JCM 7686.
OG Plasmid pAMI5 {ECO:0000313|EMBL:AGT11238.1,
OG ECO:0000313|Proteomes:UP000015480}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT11238.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT11238.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT11238.1};
RC PLASMID=Plasmid pAMI5 {ECO:0000313|Proteomes:UP000015480};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
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; CP006653; AGT11238.1; -; Genomic_DNA.
DR RefSeq; WP_020953009.1; NC_022043.1.
DR AlphaFoldDB; S5YID4; -.
DR KEGG; pami:JCM7686_pAMI5p172; -.
DR PATRIC; fig|1367847.3.peg.4208; -.
DR HOGENOM; CLU_018204_0_2_5; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000015480; Plasmid pAMI5.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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 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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}; Plasmid {ECO:0000313|EMBL:AGT11238.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT DOMAIN 4..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 120..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 227..375
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 375 AA; 39846 MW; 150780DC4E413089 CRC64;
MLLTETQEQI RDAARAFAQE RLAPGAAARD ADHAFPRAEL AEMGALGFLG MLVPEDWGGS
DLGMVAYAVA LEEIAAGDGA CSTIVSVHSS VGCMPILKYG TEAQKAEYLP RMASGDWIGG
FALTEPSTGS DAGAIKTRAV RDGDEYVING AKQFITSGKN GKVIILFAVT DPSAGKKGIS
AFIVPTDTPG YEVMSVEHKL GQHSSDTCAL AFTEMRIPAA NLLGAEGEGL KIALSNLEGG
RIGIAAQAVG MARAAFEAAR DYARDRITFG RPIIEHQAVA FKLADMATQI ATARQMVLHA
AALREAGLPC LTEASMAKLV ASEMAERVCS DAIQIHGGYG YLRDYPVERI YRDVRVCQIY
EGTSEIQRLV IARSL
//
