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Database: UniProt
Entry: A0A3N1HQB9_9ACTN
LinkDB: A0A3N1HQB9_9ACTN
Original site: A0A3N1HQB9_9ACTN 
ID   A0A3N1HQB9_9ACTN        Unreviewed;       392 AA.
AC   A0A3N1HQB9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:ROP44713.1};
GN   ORFNames=EDC03_0839 {ECO:0000313|EMBL:ROP44713.1};
OS   Pseudokineococcus lusitanus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Pseudokineococcus.
OX   NCBI_TaxID=763993 {ECO:0000313|EMBL:ROP44713.1, ECO:0000313|Proteomes:UP000276232};
RN   [1] {ECO:0000313|EMBL:ROP44713.1, ECO:0000313|Proteomes:UP000276232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7306 {ECO:0000313|EMBL:ROP44713.1,
RC   ECO:0000313|Proteomes:UP000276232};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
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:ROP44713.1}.
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DR   EMBL; RJKN01000002; ROP44713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1HQB9; -.
DR   InParanoid; A0A3N1HQB9; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000276232; 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   GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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:UP000276232}.
FT   DOMAIN          31..126
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          134..227
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          239..386
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   392 AA;  41874 MW;  414DC7EA4BB54577 CRC64;
     MTTAAGGRTP WTDPDVLSYR DLLPGPDRAR LDAAREVFDR CLRPLVPAHW DAGTFPDAAV
     AALAPLDLVA LAAEPGRALL HGLVHVELAR VDLSLSVFLG VQGVLVAEAL RRLGSDEQRA
     RYLPDLRALR RVGAFALTEP EHGSDISRHM ATTAVRSGGS WTLRGTKRWI GNGTHADHLL
     VWARDTADGE IKGFLVDRGT PGLRTSPVGP KIGLRIVQNA DVVLDDVVVG DDRLLEGATG
     FAATNDLLTS SRLWVAWQTV GLQFAAYDQA LAYTLGRVQF GRPVAATQLV QEKLVRILEN
     ATTTLGLLVR LAQLQDEGRL RAEHAALAKA SGSARMRESV AAARALLGGN GLATAHGVGR
     TFCDAEALYS YEGSHEINTL VVGRAVTGLS AF
//
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