ID A0A317DUX0_9PROT Unreviewed; 406 AA.
AC A0A317DUX0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PWR18478.1};
GN ORFNames=DKG74_18830 {ECO:0000313|EMBL:PWR18478.1};
OS Zavarzinia aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=2211142 {ECO:0000313|EMBL:PWR18478.1, ECO:0000313|Proteomes:UP000245461};
RN [1] {ECO:0000313|EMBL:PWR18478.1, ECO:0000313|Proteomes:UP000245461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AS {ECO:0000313|EMBL:PWR18478.1,
RC ECO:0000313|Proteomes:UP000245461};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-2018) 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:PWR18478.1}.
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DR EMBL; QGLE01000014; PWR18478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317DUX0; -.
DR OrthoDB; 5510711at2; -.
DR Proteomes; UP000245461; 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:SF40; ACYL-COA DEHYDROGENASE; 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:UP000245461}.
FT DOMAIN 35..147
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 151..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 256..404
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 406 AA; 44523 MW; D3D162E5E3C76C7F CRC64;
MTNRRLARRA EERDVTDQPL FDTLLREIPS PYYRPEHRGF RETLRKWVEA EIVPHVDEWD
EAGGFPRELY AKAADIGLLR LGFPEAYGGI EDTDLFHMII ATEELARAGS GGLIASLMSH
GIGAPPIVAL GSDEMKARVL PAILNGEKIS ALAITEPSGG SDVANLKTTA RREGDDYIVN
GEKVFITSGI RADYITTAVR TGGKGFGGIS LLLIDTSLPG ITRTPLKKMG WWMSDTAAIH
FDEVRVPAAN LIGPENAGFL GIVRNFNGER IALAAGANAF ARVALEEALG WARQRMTFGK
RLADHQVIRH KIVDMAQRVH ATQSMLENLA WRIEQGDAPI AEICMLKNQA TTTMEFCARE
AMQILGGAGY MRGVKTERIY REVRVNAIGG GSEEIMRDLA ARQLGL
//
