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Database: UniProt
Entry: A0A1Y1T7X6_9FLAO
LinkDB: A0A1Y1T7X6_9FLAO
Original site: A0A1Y1T7X6_9FLAO 
ID   A0A1Y1T7X6_9FLAO        Unreviewed;       454 AA.
AC   A0A1Y1T7X6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:ORL47157.1};
GN   ORFNames=IIF7_00295 {ECO:0000313|EMBL:ORL47157.1};
OS   Zunongwangia atlantica 22II14-10F7.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=1185767 {ECO:0000313|EMBL:ORL47157.1, ECO:0000313|Proteomes:UP000192746};
RN   [1] {ECO:0000313|EMBL:ORL47157.1, ECO:0000313|Proteomes:UP000192746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II14-10F7 {ECO:0000313|EMBL:ORL47157.1,
RC   ECO:0000313|Proteomes:UP000192746};
RA   Lai Q., Shao Z.;
RT   "Zunongwangia sp. 22II14-10F7 Genome Sequencing.";
RL   Submitted (APR-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:ORL47157.1}.
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DR   EMBL; ARYN01000001; ORL47157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1T7X6; -.
DR   STRING; 1185767.IIF7_00295; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000192746; 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; 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; 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.
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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192746}.
FT   DOMAIN          79..188
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          194..287
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          306..446
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   454 AA;  51202 MW;  F84E30945507B004 CRC64;
     MSFFKKVRNT VNLLKSVDMD QLAKINKQID LSEAMKTLGK LDERQLAGLM KMLKTKRKKS
     QSDLPPIDGD FYNLDYKLTE EQRELQMKVR NLMEDEIRPL INDHWNRAKF PFEIIEKFKK
     LNIAGIPYEG YGCPNLPFLM EGIIAQEIAR VDVSTSTFFG VHSGLAMGSI YLCGSEEQKQ
     KWLPQMQKLE KIGAFGLTEP NVGSGVAGGL ETTCKFDGEN WILNGQKKWI GNATFADVII
     IWARDVDSNQ VKGFLVEKDN PGFKAEKMED KMALRIVQNA IITLTDCKVA ESDRLQNANS
     FKDTANVLRM TRAGVAWQAV GCARGAYESA LKYTRKREQF GRPIASYQLV QNHLVEMVSN
     LTSMQTLCFR LSEMQDQDML TDEHASLAKV YCSMRMRDVV SRAREVMGGN GILLEHDVAR
     FVADAEAIYS YEGTKEINSL IVGRAITGYS AFVS
//
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