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Database: UniProt
Entry: K2P1S0_9FLAO
LinkDB: K2P1S0_9FLAO
Original site: K2P1S0_9FLAO 
ID   K2P1S0_9FLAO            Unreviewed;       379 AA.
AC   K2P1S0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=AcdA {ECO:0000313|EMBL:EKF54983.1};
GN   ORFNames=I215_09696 {ECO:0000313|EMBL:EKF54983.1};
OS   Galbibacter marinus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Galbibacter.
OX   NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF54983.1, ECO:0000313|Proteomes:UP000007364};
RN   [1] {ECO:0000313|EMBL:EKF54983.1, ECO:0000313|Proteomes:UP000007364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX   PubMed=23209227; DOI=10.1128/JB.01852-12;
RA   Lai Q., Li C., Shao Z.;
RT   "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL   J. Bacteriol. 194:6973-6973(2012).
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:EKF54983.1}.
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DR   EMBL; AMSG01000012; EKF54983.1; -; Genomic_DNA.
DR   RefSeq; WP_008991786.1; NZ_AMSG01000012.1.
DR   AlphaFoldDB; K2P1S0; -.
DR   STRING; 555500.I215_09696; -.
DR   PATRIC; fig|555500.3.peg.2004; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000007364; 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; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007364}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  41314 MW;  94B3EBD2E7A77203 CRC64;
     MNFDYTETQK LIAESARDFA KQFIEPYVME WDEKQIFPVD VLKKAGEFGF MGILVPEEYG
     GSGLGYHEYI AVLNEISMVD PSIGLSIAAH NSLCTNHILT FGNDEQKAKW IPKLASAEWI
     GAWGLTEHNT GSDAGGMSTT AVKEGDHWII NGAKNFITHG KSGDIAVVIV RTGEKGDSRG
     ITAFVVEKGT PGFSSGKKED KLGMRASETA EMVFTDCRIP DTNRLGPVGE GFIQSMKILD
     GGRISIGALS LGVANGAYKA ALKYSKERVQ FGKPISEFQG ISFKLADMAT DIQASELLLH
     KAAFEKNAGR PMTKIGAMCK MFASEACVRI ANEAVQIHGG YGYIKDFPVE KFYRDSKLCT
     IGEGTTEIQK VVISRHILK
//
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