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Database: UniProt
Entry: A0A1Y5SSN3_9RHOB
LinkDB: A0A1Y5SSN3_9RHOB
Original site: A0A1Y5SSN3_9RHOB 
ID   A0A1Y5SSN3_9RHOB        Unreviewed;       380 AA.
AC   A0A1Y5SSN3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acryloyl-CoA reductase (NADH) {ECO:0000313|EMBL:SLN44340.1};
DE            EC=1.3.1.95 {ECO:0000313|EMBL:SLN44340.1};
GN   Name=acrC_5 {ECO:0000313|EMBL:SLN44340.1};
GN   ORFNames=TRL7639_02352 {ECO:0000313|EMBL:SLN44340.1};
OS   Falsiruegeria litorea R37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Falsiruegeria.
OX   NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN44340.1, ECO:0000313|Proteomes:UP000193077};
RN   [1] {ECO:0000313|EMBL:SLN44340.1, ECO:0000313|Proteomes:UP000193077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN44340.1,
RC   ECO:0000313|Proteomes:UP000193077};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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; FWFO01000001; SLN44340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SSN3; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000193077; Unassembled WGS sequence.
DR   GO; GO:0043958; F:acryloyl-CoA reductase (NADH) activity; IEA:UniProtKB-EC.
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:SLN44340.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193077}.
FT   DOMAIN          6..115
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..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41239 MW;  86EEF94B1A03A1F8 CRC64;
     MDFALTEEQT AIFDMAYQFG QEHIAPFARQ WEAEGTIPKE LWPQVGELGF GGLYVSEEVG
     GSGLTRLDAT LVFEALSMAC PSVAAFLSIH NMCAKMLDSF GDDALKERIM PDVLSLNTVL
     SYCLTEPGSG SDAAALKTRA ERTNEGYTLN GTKAFISGGG YSDAYVCMVR TGEDGPKGVS
     TVYVEDGTEG LSFGGLEDKM GWKSQPTAQV QFDDCKVPAG NLVGTEGDGF KYAMMGLDGG
     RLNIASCSLG AAQTAMNLTL QYMSERQAFG KSIDQFQGLQ FRLADMEIEL QAARVFLRQA
     AWKLDQGAPD ASKHCAMAKK FVTEAGSKIV DQCLQLHGGY GYLADYGIEK LVRDLRVHQI
     LEGTNEIMRV ITARHLLANR
//
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