ACUI_RUEPO
ID ACUI_RUEPO Reviewed; 330 AA.
AC Q5LS56;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Acrylyl-CoA reductase AcuI;
DE EC=1.3.1.84;
DE AltName: Full=Acryloyl-coenzyme A reductase;
GN Name=acuI; OrderedLocusNames=SPO1914;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
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: Probably catalyzes the NADPH-dependent reduction of acrylyl-
CC CoA to propanoyl-CoA. Restores acrylate resistance when expressed in an
CC E.coli strain K12 acuI deletion. {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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By dimethylsulfonioproprionate (DMSP) and acrylate.
CC {ECO:0000269|PubMed:22563425}.
CC -!- DISRUPTION PHENOTYPE: 25-fold increased sensitivity to acrylate, growth
CC is strongly inhibited by 20 mM dimethylsulfonioproprionate (DMSP).
CC {ECO:0000269|PubMed:22563425}.
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; CP000031; AAV95191.1; -; Genomic_DNA.
DR RefSeq; WP_011047645.1; NC_003911.12.
DR PDB; 5GXE; X-ray; 1.70 A; A/B=1-330.
DR PDB; 5GXF; X-ray; 2.29 A; A/B=1-330.
DR PDBsum; 5GXE; -.
DR PDBsum; 5GXF; -.
DR AlphaFoldDB; Q5LS56; -.
DR SMR; Q5LS56; -.
DR STRING; 246200.SPO1914; -.
DR EnsemblBacteria; AAV95191; AAV95191; SPO1914.
DR KEGG; sil:SPO1914; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_26_3_5; -.
DR OMA; AQMDYNS; -.
DR OrthoDB; 884088at2; -.
DR BioCyc; MetaCyc:MON-21335; -.
DR BRENDA; 1.3.1.84; 8123.
DR Proteomes; UP000001023; Chromosome.
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; 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; 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 3D-structure; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..330
FT /note="Acrylyl-CoA reductase AcuI"
FT /id="PRO_0000420615"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 159..162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:5GXE"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5GXE"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5GXE"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:5GXE"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5GXE"
SQ SEQUENCE 330 AA; 34450 MW; F6F52088CE1EEA67 CRC64;
MFNALVVDKD EESGKTQAAV KQLSLTDLPV GEVTVAVEYS TVNYKDGLCI GPGGGLVRKY
PHVPGIDFAG TVENSSDERY KPGDKVVLTG WRVGEAHWGG YSQKANVRAD WLVPLPEGLD
TRQAMAVGTA GFTAMLAVMA LEDHGLTPGH GPVLVTGAAG GVGSVATAIL AHLGYEVAAV
TGRPETADYL TSLGATQIVA RDEINETVKR PLESEIWAGC VDAVGGAMLA RVLGQMKYGA
SVAAVGLAGG AGLPATVIPF LLRGVNLLGI DSVMQPYANR LRAWERIARD LPMDKLEAMI
RPATLSDLPG LGADILKGQV QGRVVVDVNA
