ID M9RFI8_9RHOB Unreviewed; 560 AA.
AC M9RFI8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AGI70493.1};
GN ORFNames=OA238_c02240 {ECO:0000313|EMBL:AGI70493.1};
OS Octadecabacter arcticus 238.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI70493.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI70493.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI70493.1,
RC ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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; CP003742; AGI70493.1; -; Genomic_DNA.
DR RefSeq; WP_015493734.1; NC_020908.1.
DR AlphaFoldDB; M9RFI8; -.
DR STRING; 391616.OA238_c02240; -.
DR KEGG; oar:OA238_c02240; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_5_5; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000004688; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF25; ACYL-COA DEHYDROGENASE; 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 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000004688}.
FT DOMAIN 179..290
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 296..397
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 411..560
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 560 AA; 61373 MW; F6FC1D08476255D4 CRC64;
MPRDAHDQNA KSTPVLPDLL ATTAATIAPL RALLETAKDC VRDKVMVDGR ASGALVEAEQ
TAAHGLAWLA TYVEALAQMQ VWAEKLLADS KFGEVEQLIH QIAFGEYLWQ IYGGIPMNQG
EILRLQDIGL TQDQMRIMME PSVKALTQHA NTQAARLRLV DLMQERSAEV TVGATGLDDE
LDMIREQFRR YAVEKVEPFA HEWHLKDELI PTSVIDELAE MGVFGLTIPE EYGGLGLSKA
SMCVVSEELS RGYIGVGSLG TRTEIAAELI IAGGTEEQKQ KWLPALASAE KLPTAVFTEP
NTGSDLGALR ARAVKDGDDY RVTGNKTWIT HASRTHVMTL LARTNPDSSD YKGLSMFLAE
KTPGDDAHPF PTEGMTGGEI EVLGYRGMKE HELAFDNFHV KGENLLGGEE GKGFKQLMET
FESARIQTAA RAIGVACSAL DVAMQYAQDR KQFGKSLIEF PRVANKLAMM AVEIMIARQL
TYFSAFEKDE GRRCDVEAGM AKLLGARVAW AAADNALQIH GGNGFALEYK VSRILCDARI
LNIFEGAAEI QAQVIARRIL
//
