ACUI_ECOLI
ID ACUI_ECOLI Reviewed; 324 AA.
AC P26646; Q2M8W1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable acrylyl-CoA reductase AcuI;
DE EC=1.3.1.84;
DE AltName: Full=Acryloyl-coenzyme A reductase AcuI;
GN Name=acuI; Synonyms=yhdH; OrderedLocusNames=b3253, JW3222;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1370469; DOI=10.1016/s0021-9258(18)48362-7;
RA Li S.-J., Cronan J.E. Jr.;
RT "The gene encoding the biotin carboxylase subunit of Escherichia coli
RT acetyl-CoA carboxylase.";
RL J. Biol. Chem. 267:855-863(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=K12 / BW25113;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=15388933; DOI=10.1107/s0907444904020220;
RA Sulzenbacher G., Roig-Zamboni V., Pagot F., Grisel S., Salomoni A.,
RA Valencia C., Campanacci V., Vincentelli R., Tegoni M., Eklund H.,
RA Cambillau C.;
RT "Structure of Escherichia coli YhdH, a putative quinone oxidoreductase.";
RL Acta Crystallogr. D 60:1855-1862(2004).
CC -!- FUNCTION: Probably catalyzes the NADPH-dependent reduction of acrylyl-
CC CoA to propanoyl-CoA. {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:0000269|PubMed:15388933}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: 100-fold increased sensitivity to acrylate, about
CC 8-fold increased sensitivity to 3-hydroxypropionate. Acrylate is
CC bacteriostatic, not bacteriocidal. Can be complemented by acuI from a
CC number of other bacteria, including Rhodobacter sphaeroides strain
CC 2.4.1 (AC Q3J6K9) and Ruegeria pomeyroi (AC Q5LS56).
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; M80458; AAA23407.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58056.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76285.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77295.1; -; Genomic_DNA.
DR PIR; JS0688; JS0688.
DR RefSeq; NP_417719.1; NC_000913.3.
DR RefSeq; WP_001148481.1; NZ_SSZK01000034.1.
DR PDB; 1O89; X-ray; 2.25 A; A=2-324.
DR PDB; 1O8C; X-ray; 2.60 A; A/B/C/D=2-324.
DR PDBsum; 1O89; -.
DR PDBsum; 1O8C; -.
DR AlphaFoldDB; P26646; -.
DR SMR; P26646; -.
DR BioGRID; 4261942; 8.
DR BioGRID; 852159; 1.
DR DIP; DIP-12295N; -.
DR IntAct; P26646; 6.
DR STRING; 511145.b3253; -.
DR SWISS-2DPAGE; P26646; -.
DR jPOST; P26646; -.
DR PaxDb; P26646; -.
DR PRIDE; P26646; -.
DR EnsemblBacteria; AAC76285; AAC76285; b3253.
DR EnsemblBacteria; BAE77295; BAE77295; BAE77295.
DR GeneID; 947848; -.
DR KEGG; ecj:JW3222; -.
DR KEGG; eco:b3253; -.
DR PATRIC; fig|1411691.4.peg.3476; -.
DR EchoBASE; EB1291; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_26_3_6; -.
DR InParanoid; P26646; -.
DR OMA; AQMDYNS; -.
DR PhylomeDB; P26646; -.
DR BioCyc; EcoCyc:EG11315-MON; -.
DR BioCyc; MetaCyc:EG11315-MON; -.
DR BRENDA; 1.3.1.84; 2026.
DR EvolutionaryTrace; P26646; -.
DR PRO; PR:P26646; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043957; F:acryloyl-CoA reductase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 3D-structure; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..324
FT /note="Probable acrylyl-CoA reductase AcuI"
FT /id="PRO_0000169493"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 156..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 178..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 242
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT BINDING 313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15388933"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1O8C"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1O89"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 118..140
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:1O8C"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1O89"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:1O89"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:1O89"
SQ SEQUENCE 324 AA; 34724 MW; ED1F71ECA0BDE0C1 CRC64;
MQALLLEQQD GKTLASVQTL DESRLPEGDV TVDVHWSSLN YKDALAITGK GKIIRNFPMI
PGIDFAGTVR TSEDPRFHAG QEVLLTGWGV GENHWGGLAE QARVKGDWLV AMPQGLDARK
AMIIGTAGFT AMLCVMALED AGVRPQDGEI VVTGASGGVG STAVALLHKL GYQVVAVSGR
ESTHEYLKSL GASRVLPRDE FAESRPLEKQ VWAGAIDTVG DKVLAKVLAQ MNYGGCVAAC
GLAGGFTLPT TVMPFILRNV RLQGVDSVMT PPERRAQAWQ RLVADLPESF YTQAAKEISL
SEAPNFAEAI INNQIQGRTL VKVN
