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Database: UniProt
Entry: W9GJ55_9MICO
LinkDB: W9GJ55_9MICO
Original site: W9GJ55_9MICO 
ID   W9GJ55_9MICO            Unreviewed;       386 AA.
AC   W9GJ55;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EWT06276.1};
GN   ORFNames=N864_22705 {ECO:0000313|EMBL:EWT06276.1};
OS   Intrasporangium chromatireducens Q5-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT06276.1, ECO:0000313|Proteomes:UP000019494};
RN   [1] {ECO:0000313|Proteomes:UP000019494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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:EWT06276.1}.
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DR   EMBL; AWQS01000056; EWT06276.1; -; Genomic_DNA.
DR   RefSeq; WP_034715805.1; NZ_AWQS01000056.1.
DR   AlphaFoldDB; W9GJ55; -.
DR   PATRIC; fig|584657.3.peg.1811; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000019494; Unassembled WGS sequence.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019494}.
FT   DOMAIN          6..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  41975 MW;  104E6E8DEE15673B CRC64;
     MSKLSADEQD MVRLVAEFVD ERVRPRVREF EAEDLYPEEL IEEMKKLGFF GLLVPSEHGG
     VDVSTSCFAQ VTAELARGWM SLAGAIGGHS VITFLVRHFG TPEQQAAYLP RMADGSLRAT
     MALTEPSGGS DLQGMRTHAD RDGDDLVITG SKTWISNAQH AGLIGLLCLT DRDAKPAHRG
     MSVVLVEPGE GLTISSKIPK LGYRGVEACE LTFDAMRVPA SAVLGGEANR GWGHMMRGLE
     VGRVQVAARA LGVGQAALDD ALTYAQTRES FGKPIWRHQS VGNLLADMAT KLHAARLLTI
     DAAERLDEGR RADMEAGMAK LFASETAMQV ALDAIRVHGG YGYSKEYDVE RYFRDAPLMI
     VGEGTNEIQR NVIAAQLVAR DKDRSM
//
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