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Database: UniProt
Entry: A0A0A0EIM8_9RHOB
LinkDB: A0A0A0EIM8_9RHOB
Original site: A0A0A0EIM8_9RHOB 
ID   A0A0A0EIM8_9RHOB        Unreviewed;       388 AA.
AC   A0A0A0EIM8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGM49958.1};
GN   ORFNames=ATO9_00160 {ECO:0000313|EMBL:KGM49958.1};
OS   Pseudooceanicola atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM49958.1, ECO:0000313|Proteomes:UP000030004};
RN   [1] {ECO:0000313|EMBL:KGM49958.1, ECO:0000313|Proteomes:UP000030004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s11g {ECO:0000313|EMBL:KGM49958.1,
RC   ECO:0000313|Proteomes:UP000030004};
RX   PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA   Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT   "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT   seawater of the Atlantic Ocean and reclassification of Oceanicola
RT   batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT   nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT   Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT   Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT   comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT   flagellatus comb. nov.";
RL   Antonie Van Leeuwenhoek 107:1065-1074(2015).
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:KGM49958.1}.
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DR   EMBL; AQQX01000001; KGM49958.1; -; Genomic_DNA.
DR   RefSeq; WP_043743508.1; NZ_CP051248.1.
DR   AlphaFoldDB; A0A0A0EIM8; -.
DR   STRING; 1461694.ATO9_00160; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000030004; 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:UP000030004}.
FT   DOMAIN          9..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   388 AA;  42166 MW;  AE3DFAF2B3852397 CRC64;
     MAMDDDSFEQ VLDTVSRFAR DRLIPAETKV EELDDIPEDI VQDMRDLGLF GLSIPESFGG
     LELTTLQESQ VVEALCYASM SFRSLVGTNV GIGAQGIVME GTDAQKEQYL PGLASGELIA
     SFALTEPDNG SDASHIRTSA RKDGSDYVIN GTKRYITNAV RANVFTLFAR TNPDDPGAGG
     VSAFLVPADT PGITIATPDR KMGQKGTKTS DVILEDVRIP EEFIVGGPQN LNRGFRTAMK
     VLDRGRIHVS SMAVGTAQRM LDEALGYAME RKQFNVPICE HQLVQGLLAD SQAELAAGRA
     LVRETARKYD ATGAVALEAS CAKYFCTEMA GRVADRAVQV HGGAGYMAEY PIERLYRDAR
     LLRIYEGTSQ IQQIIIARNI IKAAAQRM
//
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