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Database: UniProt
Entry: A0A2Z2NT23_9GAMM
LinkDB: A0A2Z2NT23_9GAMM
Original site: A0A2Z2NT23_9GAMM 
ID   A0A2Z2NT23_9GAMM        Unreviewed;       381 AA.
AC   A0A2Z2NT23;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ASJ72888.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:ASJ72888.1};
GN   Name=acdA_3 {ECO:0000313|EMBL:ASJ72888.1};
GN   ORFNames=IMCC3135_14015 {ECO:0000313|EMBL:ASJ72888.1};
OS   Granulosicoccus antarcticus IMCC3135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Granulosicoccaceae; Granulosicoccus.
OX   NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ72888.1, ECO:0000313|Proteomes:UP000250079};
RN   [1] {ECO:0000313|EMBL:ASJ72888.1, ECO:0000313|Proteomes:UP000250079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ72888.1,
RC   ECO:0000313|Proteomes:UP000250079};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; CP018632; ASJ72888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2NT23; -.
DR   KEGG; gai:IMCC3135_14015; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000250079; 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; 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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
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   ECO:0000313|EMBL:ASJ72888.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000250079}.
FT   DOMAIN          6..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   381 AA;  41266 MW;  AA7D0E22F562A3B0 CRC64;
     MNFELTEEQR AIQDMALAFG EAEIAPHAAR WEQEGSIPKE LLRQVGELGF AGIYVSEEFG
     GSNLSRLDAT LIFEALSKAC PSVAAFISIH NMCAWMIDRY GSDEMRARLL PSLCSYEKVA
     SYCLTEPGSG SDAAALRTRA EKVGDNLSLN GSKAFISGGG YADLYLVMCR TGGEGPSGIS
     AVLVEDGTPG LSFGAPERKM GWRSQPTAEV QFADCQVPAS NLLGKEGDGF RYAMSGLDGG
     RLNISACSLG AAQNAMDKSV VYASERKAFG APINQLQSLQ FKLADMEISL QASRSLLHKA
     AWKLDQKAPD AAKFCAMAKR FVTDQCFDVA NDALQIHGGY GYLEDYGIEK IVRDIRVHQI
     LEGTNEIMRL VTARALMSEY T
//
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