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Database: UniProt
Entry: A0A081K8F5_9GAMM
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ID   A0A081K8F5_9GAMM        Unreviewed;       390 AA.
AC   A0A081K8F5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Isovaleryl-CoA dehydrogenase {ECO:0000313|EMBL:KEI70431.1};
GN   ORFNames=GV64_06505 {ECO:0000313|EMBL:KEI70431.1};
OS   Endozoicomonas elysicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI70431.1, ECO:0000313|Proteomes:UP000027997};
RN   [1] {ECO:0000313|EMBL:KEI70431.1, ECO:0000313|Proteomes:UP000027997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI70431.1,
RC   ECO:0000313|Proteomes:UP000027997};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) 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:KEI70431.1}.
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DR   EMBL; JOJP01000001; KEI70431.1; -; Genomic_DNA.
DR   RefSeq; WP_034844086.1; NZ_JOJP01000001.1.
DR   AlphaFoldDB; A0A081K8F5; -.
DR   STRING; 305900.GV64_06505; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000027997; 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; 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.
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:UP000027997}.
FT   DOMAIN          9..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..388
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   390 AA;  43168 MW;  8FB270E6B712985E CRC64;
     MTASQFNLTT EQQSLLDHAD RFGREQLFPY AARMDNEEWW PQDVFKQFGE LGFLGVTIPE
     EYGGAGMSML EAGLILQGFS RWNHALALSW VAHDNLCANN IYNNGSEYLR EQYLPKLCSG
     EWIGCLGLTE PGAGSDALGS MRTKAIRDGD EYVLNGSKIY ITNGPVADVC LVYAKTEPGK
     GSKGITAFVV ETSWPGFKVA QKLDKMGFRG SQTAELVFED LRVPVKNIVG KEHQGHQVVM
     SGLDFERSMI APINTGIAER ALDLSIDYAG TRQQFGKPIA SFQMVQARIA DMYVWVETMK
     TFCWKVLAEV SEVDETQAGR GEIHARTAAS VMYCADMSNK VLDNAVQVHG GTGYIWESEI
     NRLFRSTKLL EIGAGTTEVR KMIIAGELLK
//
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