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Database: UniProt
Entry: A0A0N1BME2_9PROT
LinkDB: A0A0N1BME2_9PROT
Original site: A0A0N1BME2_9PROT 
ID   A0A0N1BME2_9PROT        Unreviewed;       388 AA.
AC   A0A0N1BME2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KPF77462.1};
GN   ORFNames=IP88_06250 {ECO:0000313|EMBL:KPF77462.1};
OS   alpha proteobacterium AAP81b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF77462.1, ECO:0000313|Proteomes:UP000037971};
RN   [1] {ECO:0000313|EMBL:KPF77462.1, ECO:0000313|Proteomes:UP000037971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP81b {ECO:0000313|EMBL:KPF77462.1,
RC   ECO:0000313|Proteomes:UP000037971};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF77462.1}.
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DR   EMBL; LJHX01000055; KPF77462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1BME2; -.
DR   STRING; 1523432.IP88_06250; -.
DR   PATRIC; fig|1523432.3.peg.2480; -.
DR   OrthoDB; 7795946at2; -.
DR   Proteomes; UP000037971; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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; 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; 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:UP000037971}.
FT   DOMAIN          15..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..222
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          237..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   388 AA;  42391 MW;  A890AD9A7B69F4D4 CRC64;
     MTLQTFTDEP AHVGELRRTV ARFVAAHAPR EKRIAWDKAH DWPRDVYAEF NKLGLTALTI
     PEAHGGAGQD IVAAIAVIEE LAQAGPALAG PYIHTAFYGG LNLSENGSDA QKAEYLPRLA
     RGELFFAYGL SEPDVGGDLA SVTTRARLEG DEVVIDGAKR WCSGADWADV LYTLVRSGPA
     EDRYRNLSFV LVPRTTPGVT MQPIEHANLR YMASQDVFFD QVRVPAANIV GGESMWNQGW
     KILAGRALDV EKLEITAVAL GIARAAVTEA WDYAQSRIQF GKPIAQHQAI RHKLVTARTK
     LQAARHMLYH AAWLAGEGRP CSIETSMAKL FVADTGVEIA LICQQVMGAY GLSDAFDMER
     HVRDLLGMPI VGGSSDMQKN NLAGLWKL
//
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