ACUI_CERS4
ID ACUI_CERS4 Reviewed; 326 AA.
AC Q3J6K9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Acrylyl-CoA reductase AcuI;
DE EC=1.3.1.84;
DE AltName: Full=Acryloyl-coenzyme A reductase;
GN Name=acuI; OrderedLocusNames=RHOS4_00070; ORFNames=RSP_1434;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=22056933; DOI=10.1128/jb.05959-11;
RA Schneider K., Asao M., Carter M.S., Alber B.E.;
RT "Rhodobacter sphaeroides uses a reductive route via propionyl coenzyme A to
RT assimilate 3-hydroxypropionate.";
RL J. Bacteriol. 194:225-232(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=21249136; DOI=10.1371/journal.pone.0015972;
RA Sullivan M.J., Curson A.R., Shearer N., Todd J.D., Green R.T.,
RA Johnston A.W.;
RT "Unusual regulation of a leaderless operon involved in the catabolism of
RT dimethylsulfoniopropionate in Rhodobacter sphaeroides.";
RL PLoS ONE 6:E15972-E15972(2011).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=22563425; DOI=10.1371/journal.pone.0035947;
RA Todd J.D., Curson A.R., Sullivan M.J., Kirkwood M., Johnston A.W.;
RT "The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and
RT resembles yhdH of E. coli and other bacteria in conferring resistance to
RT acrylate.";
RL PLoS ONE 7:E35947-E35947(2012).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of acrylyl-CoA to
CC propanoyl-CoA. Is essential for growth with 3-hydroxypropanoate as a
CC sole carbon source. Restores acrylate resistance when expressed in the
CC E.coli strain K12 acuI deletion. {ECO:0000269|PubMed:22056933,
CC ECO:0000269|PubMed:22563425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:26454, ChEBI:CHEBI:15378, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.84;
CC Evidence={ECO:0000269|PubMed:22056933};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Moderately induced by acrylate and
CC dimethylsulfonioproprionate (DMSP), as well as by 3-hydroxypropanoate.
CC Part of the acuR-acuI-dddL operon. {ECO:0000269|PubMed:21249136}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to acrylate on plates,
CC decreased ability to degrade acrylate (PubMed:21249136). No effect
CC during photoheterotropic (anaerobic/light) growth on succinate, no
CC growth on 3-hydroxypropionate under the same conditions. Loss of 3-
CC hydroxypropanoate and acrylate-dependent oxidation of NADPH
CC (PubMed:22056933). {ECO:0000269|PubMed:21249136,
CC ECO:0000269|PubMed:22056933}.
CC -!- MISCELLANEOUS: The zinc-binding residues of the alcohol dehydrogenase
CC family are not conserved.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Acrylyl-CoA reductase subfamily. {ECO:0000305}.
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DR EMBL; JQ582462; AFD36450.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA77575.1; -; Genomic_DNA.
DR RefSeq; WP_011336735.1; NZ_CP030271.1.
DR RefSeq; YP_351476.1; NC_007493.2.
DR AlphaFoldDB; Q3J6K9; -.
DR SMR; Q3J6K9; -.
DR STRING; 272943.RSP_1434; -.
DR EnsemblBacteria; ABA77575; ABA77575; RSP_1434.
DR KEGG; rsp:RSP_1434; -.
DR PATRIC; fig|272943.9.peg.298; -.
DR eggNOG; COG0604; Bacteria.
DR OMA; GVVREYP; -.
DR PhylomeDB; Q3J6K9; -.
DR BRENDA; 1.3.1.84; 5383.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043957; F:acryloyl-CoA reductase (NADP+) activity; IEA:UniProtKB-EC.
DR InterPro; IPR014188; Acrylyl-CoA_reductase_AcuI.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43677:SF1; PTHR43677:SF1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02823; oxido_YhdH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..326
FT /note="Acrylyl-CoA reductase AcuI"
FT /id="PRO_0000420614"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 178..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 34165 MW; 35B371FA875CEE83 CRC64;
MRAVLIEKSD DTQSVSVTEL AEDQLPEGDV LVDVAYSTLN YKDALAITGK APVVRRFPMV
PGIDFTGTVA QSSHADFKPG DRVILNGWGV GEKHWGGLAE RARVRGDWLV PLPAPLDLRQ
AAMIGTAGYT AMLCVLALER HGVVPGNGEI VVSGAAGGVG SVATTLLAAK GYEVAAVTGR
ASEAEYLRGL GAASVIDRNE LTGKVRPLGQ ERWAGGIDVA GSTVLANMLS MMKYRGVVAA
CGLAAGMDLP ASVAPFILRG MTLAGVDSVM CPKTDRLAAW ARLASDLDPA KLEEMTTELP
FSEVIETAPK FLDGTVRGRI VIPVTP
