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Database: UniProt
Entry: A0A075KF80_9FIRM
LinkDB: A0A075KF80_9FIRM
Original site: A0A075KF80_9FIRM 
ID   A0A075KF80_9FIRM        Unreviewed;       379 AA.
AC   A0A075KF80;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AIF52715.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:AIF52715.1};
GN   ORFNames=UFO1_3172 {ECO:0000313|EMBL:AIF52715.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF52715.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF52715.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF52715.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(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; CP008852; AIF52715.1; -; Genomic_DNA.
DR   RefSeq; WP_038672361.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075KF80; -.
DR   STRING; 484770.UFO1_3172; -.
DR   KEGG; puf:UFO1_3172; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_9; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000027983; Chromosome.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 1.
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; PS00072; ACYL_COA_DH_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027983}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  40809 MW;  BC482A6636969699 CRC64;
     MNFVLTQEQE DIRKMVRAFA EKSVAPTAAE RDEKEYFPRD IFDQMGELGI LGLPYPEEYG
     GAGSDFLSYS IAVEEISRVC ASTGIGLSVH VSLASWPIFK YGTEEQKQKY LRALAEGTKL
     GAFGLTEPNA GTDAAAATTV AVRDGDSYIL NGSKIFNTNG GEAEIEVIFA STDKTAGLKG
     LSAFIVEKGT PGLSFGKKEV KMGIRSSVQR EVIMENCRVP AENLLGKEGG GFKIAMTSLD
     GGRIGVASQA VGIAQGALEQ AIQYSKARIQ FGKPIANNQA IAFKIADMAA KVEAARLLTY
     KAAYHKSHEL PYSKEAAMAK LVASDAAMAV TTEAVQIFGG YGFSREYPVE RMMRDAKITQ
     IYEGTNEVQR MVISGAVLR
//
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