ID W8VXW3_9FLAO Unreviewed; 602 AA.
AC W8VXW3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:BAO56627.1};
GN ORFNames=NMS_2618 {ECO:0000313|EMBL:BAO56627.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO56627.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO56627.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO56627.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(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; AP014548; BAO56627.1; -; Genomic_DNA.
DR RefSeq; WP_041497132.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VXW3; -.
DR STRING; 1454201.NMS_2618; -.
DR HOGENOM; CLU_018204_3_3_10; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000031760; Chromosome.
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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_C; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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}.
FT DOMAIN 33..146
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 150..245
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 257..419
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 470..573
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 602 AA; 66428 MW; FE7DD5EFDCE34AB0 CRC64;
MSNETAEKKM IRGGQFIVTE TAAEDVFTPE DFSDEQQMMK ESVREFVDKE IVPHKERFEK
KDYALTEEVM RKAGEMGFLG IAVPEEYDGL GMGFVSTMLV CDYISGATGS IATAFGAHTG
IGTMPITLYG TEEQKKKYVP KLATGEWFGA YCLTEPGAGS DANSGKTKAE LTEDGKHYKI
NGQKMWISNA GFCNVFVVFA RMGDDKNITG FIVENDPSNG ISMGEEEHKL GIHSSSTRQV
FFNDCLVPVE NMLAGQGEGF KIAMNALNVG RIKLAAACLD AQRRVISLAT QYANDREQFN
TPIAKFGAIR KKIADMATNA YVGESASYRA AKGIENRIHA RQEAGETFAQ SELKGVEEFA
IECSILKVAV SEDMQECADE GIQIYGGMGF SADAPMEAAW RDARISRIYE GTNEINRMLA
VGMLVKKAMK GHVNLLEPAM AVGQELTSIP SFDTPDYSQL FAEEKEMLAK LKKVFLMVAG
SAVQKLGTEL EKHQQLLLAA SDILIEIYMA ESAILRTEKN VNRSSEEAQK EQIAMSKLYL
YKASKVIQAK AEEGIAGFAE GDEQRMMLMG LKRFTKYANL PNVIELRNTI ADKVTEENKY
PF
//
