ID A0A1X6Z0Q7_9RHOB Unreviewed; 386 AA.
AC A0A1X6Z0Q7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acryloyl-CoA reductase (NADH) {ECO:0000313|EMBL:SLN36570.1};
DE EC=1.3.1.95 {ECO:0000313|EMBL:SLN36570.1};
GN Name=acrC_1 {ECO:0000313|EMBL:SLN36570.1};
GN ORFNames=RUM8411_01573 {ECO:0000313|EMBL:SLN36570.1};
OS Ruegeria meonggei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1446476 {ECO:0000313|EMBL:SLN36570.1, ECO:0000313|Proteomes:UP000193778};
RN [1] {ECO:0000313|EMBL:SLN36570.1, ECO:0000313|Proteomes:UP000193778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8411 {ECO:0000313|EMBL:SLN36570.1,
RC ECO:0000313|Proteomes:UP000193778};
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; FWFP01000004; SLN36570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6Z0Q7; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000193778; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF43; 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 PIRSF; PIRSF016578; HsaA; 3.
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:SLN36570.1}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 121..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 43215 MW; 3BFA592205B29DFC CRC64;
MQFGLSEEQD MIVSTVRSFV ENEIYPHEAK VERTGTVPAE LGEEIKQKCI DLGFYACNFP
EEVGGAGLSH LDFTLVEREL GRGSMALTHF FGRPQNILMA CNEDQRARYL LPAVRGERMD
ALAMTEPDAG SDVRGMNCQA VRDGGDWVVN GSKHFISGAE HADFFIVFIA TGVDETPKGP
KKRITTFLVD RGTPGFEVRE GYNSVSHKGY KNYILYFDNC RLPDAQVLGE VDGGFAVMNE
WLYATRLTVA AFSVGRARRC FDYALNYAAE RKQFGQPIGK FQGVGFQIAD MITEIDAADW
LTLSAAWRLD QSLPANREIA SAKLYASEML ARVTDTTLQI FGGMGLMDDF PIERFWRDAR
VERIWDGTSE IQRHIISRDL LRPLGA
//
