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Database: UniProt
Entry: D8F1D1_9DELT
LinkDB: D8F1D1_9DELT
Original site: D8F1D1_9DELT 
ID   D8F1D1_9DELT            Unreviewed;       401 AA.
AC   D8F1D1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative butyryl-CoA dehydrogenase {ECO:0000313|EMBL:EFK10372.1};
GN   ORFNames=NPH_3488 {ECO:0000313|EMBL:EFK10372.1};
OS   delta proteobacterium NaphS2.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK10372.1, ECO:0000313|Proteomes:UP000003834};
RN   [1] {ECO:0000313|EMBL:EFK10372.1, ECO:0000313|Proteomes:UP000003834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NaphS2 {ECO:0000313|EMBL:EFK10372.1,
RC   ECO:0000313|Proteomes:UP000003834};
RX   PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA   Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA   Lipton M.S., Deboy R., Methe B.A.;
RT   "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT   Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL   PLoS ONE 5:E14072-E14072(2010).
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:EFK10372.1}.
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DR   EMBL; ADZZ01000218; EFK10372.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8F1D1; -.
DR   OrthoDB; 9765339at2; -.
DR   Proteomes; UP000003834; 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; 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   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:UP000003834}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..222
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..388
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   401 AA;  44833 MW;  25EF6BDEFA391B02 CRC64;
     MDFELTREQK DIKKAAAEFA QGEFDKDFIL LCEADHRFPR EIYQKAGELG FIGLDYSEDV
     GGGGLGVMEN VLVIEAFCKA DSGMGMAIHL AYLPAKIVKK FGTPPQRKKF LTPLVAGKWV
     SAVSFTEPDH GSDLTRMETT LEEEADGFVL NGTKIFTTNG KYADFFIVLA QEDPNAGPGK
     GMSTILVERD SNSWLGGNME INEITGKMGL RMTSSSEVVF HDLKIPRENI LGERGRGLMN
     VLEFLDESRI EIGAQALGNC EGAFLKALAH ARERKQFNRP IIDFQGVGHK LARMWSRIQS
     LKWLNYYGAW LCDKGPARLS RSIPLITSVV KHHVPETAKA IIDDAITVFG GYGYFLDQEV
     ERRYRDNRIV EVYEGTVEVQ LNNIVRVLGK MPLPFLDTEL L
//
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