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Protein

Probable acrylyl-CoA reductase AcuI

Gene

acuI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA.1 Publication

Catalytic activityi

Propanoyl-CoA + NADP+ = acrylyl-CoA + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411NADP; via amide nitrogen1 Publication
Binding sitei198 – 1981NADP1 Publication
Binding sitei242 – 2421NADP; via amide nitrogen1 Publication
Binding sitei256 – 2561NADP; via carbonyl oxygen1 Publication
Binding sitei267 – 2671NADP1 Publication
Binding sitei313 – 3131NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 1594NADP1 Publication
Nucleotide bindingi178 – 1803NADP1 Publication

GO - Molecular functioni

  • acryloyl-CoA reductase (NADP+) activity Source: EcoCyc
  • zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:EG11315-MONOMER.
ECOL316407:JW3222-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable acrylyl-CoA reductase AcuI (EC:1.3.1.84)
Alternative name(s):
Acryloyl-coenzyme A reductase AcuI
Gene namesi
Name:acuI
Synonyms:yhdH
Ordered Locus Names:b3253, JW3222
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11315. acuI.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

100-fold increased sensitivity to acrylate, about 8-fold increased sensitivity to 3-hydroxypropionate. Acrylate is bacteriostatic, not bacteriocidal. Can be complemented by acuI from a number of other bacteria, including Rhodobacter sphaeroides strain 2.4.1 (AC Q3J6K9) and Ruegeria pomeyroi (AC Q5LS56).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Probable acrylyl-CoA reductase AcuIPRO_0000169493Add
BLAST

Proteomic databases

EPDiP26646.
PaxDbiP26646.
PRIDEiP26646.

2D gel databases

SWISS-2DPAGEP26646.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4261942. 8 interactions.
DIPiDIP-12295N.
IntActiP26646. 6 interactions.
STRINGi511145.b3253.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi14 – 196Combined sources
Helixi22 – 243Combined sources
Beta strandi29 – 3810Combined sources
Helixi41 – 488Combined sources
Helixi50 – 523Combined sources
Beta strandi56 – 594Combined sources
Beta strandi63 – 7210Combined sources
Beta strandi82 – 865Combined sources
Turni88 – 925Combined sources
Beta strandi97 – 1048Combined sources
Helixi106 – 1083Combined sources
Helixi118 – 14023Combined sources
Helixi145 – 1473Combined sources
Beta strandi149 – 1546Combined sources
Helixi158 – 16912Combined sources
Beta strandi174 – 1796Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 1907Combined sources
Beta strandi192 – 1976Combined sources
Helixi198 – 2003Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi212 – 2198Combined sources
Helixi221 – 2299Combined sources
Beta strandi231 – 2399Combined sources
Beta strandi246 – 2527Combined sources
Helixi253 – 2586Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi267 – 2693Combined sources
Helixi272 – 28514Combined sources
Helixi288 – 2914Combined sources
Beta strandi296 – 2983Combined sources
Helixi300 – 3023Combined sources
Helixi303 – 3119Combined sources
Beta strandi319 – 3224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O89X-ray2.25A2-324[»]
1O8CX-ray2.60A/B/C/D2-324[»]
ProteinModelPortaliP26646.
SMRiP26646. Positions 2-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26646.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D3Z. Bacteria.
COG0604. LUCA.
HOGENOMiHOG000294662.
InParanoidiP26646.
KOiK19745.
OMAiAQMDYNS.
OrthoDBiEOG6V4G9J.
PhylomeDBiP26646.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014188. Acrylyl-CoA_reductase_AcuI.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF13. PTHR11695:SF13. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02823. oxido_YhdH. 1 hit.

Sequencei

Sequence statusi: Complete.

P26646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQALLLEQQD GKTLASVQTL DESRLPEGDV TVDVHWSSLN YKDALAITGK
60 70 80 90 100
GKIIRNFPMI PGIDFAGTVR TSEDPRFHAG QEVLLTGWGV GENHWGGLAE
110 120 130 140 150
QARVKGDWLV AMPQGLDARK AMIIGTAGFT AMLCVMALED AGVRPQDGEI
160 170 180 190 200
VVTGASGGVG STAVALLHKL GYQVVAVSGR ESTHEYLKSL GASRVLPRDE
210 220 230 240 250
FAESRPLEKQ VWAGAIDTVG DKVLAKVLAQ MNYGGCVAAC GLAGGFTLPT
260 270 280 290 300
TVMPFILRNV RLQGVDSVMT PPERRAQAWQ RLVADLPESF YTQAAKEISL
310 320
SEAPNFAEAI INNQIQGRTL VKVN
Length:324
Mass (Da):34,724
Last modified:August 1, 1992 - v1
Checksum:iED1F71ECA0BDE0C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80458 Genomic DNA. Translation: AAA23407.1.
U18997 Genomic DNA. Translation: AAA58056.1.
U00096 Genomic DNA. Translation: AAC76285.1.
AP009048 Genomic DNA. Translation: BAE77295.1.
PIRiJS0688.
RefSeqiNP_417719.1. NC_000913.3.
WP_001148481.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76285; AAC76285; b3253.
BAE77295; BAE77295; BAE77295.
GeneIDi947848.
KEGGiecj:JW3222.
eco:b3253.
PATRICi32121932. VBIEscCol129921_3350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80458 Genomic DNA. Translation: AAA23407.1.
U18997 Genomic DNA. Translation: AAA58056.1.
U00096 Genomic DNA. Translation: AAC76285.1.
AP009048 Genomic DNA. Translation: BAE77295.1.
PIRiJS0688.
RefSeqiNP_417719.1. NC_000913.3.
WP_001148481.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O89X-ray2.25A2-324[»]
1O8CX-ray2.60A/B/C/D2-324[»]
ProteinModelPortaliP26646.
SMRiP26646. Positions 2-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261942. 8 interactions.
DIPiDIP-12295N.
IntActiP26646. 6 interactions.
STRINGi511145.b3253.

2D gel databases

SWISS-2DPAGEP26646.

Proteomic databases

EPDiP26646.
PaxDbiP26646.
PRIDEiP26646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76285; AAC76285; b3253.
BAE77295; BAE77295; BAE77295.
GeneIDi947848.
KEGGiecj:JW3222.
eco:b3253.
PATRICi32121932. VBIEscCol129921_3350.

Organism-specific databases

EchoBASEiEB1291.
EcoGeneiEG11315. acuI.

Phylogenomic databases

eggNOGiENOG4105D3Z. Bacteria.
COG0604. LUCA.
HOGENOMiHOG000294662.
InParanoidiP26646.
KOiK19745.
OMAiAQMDYNS.
OrthoDBiEOG6V4G9J.
PhylomeDBiP26646.

Enzyme and pathway databases

BioCyciEcoCyc:EG11315-MONOMER.
ECOL316407:JW3222-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP26646.
PROiP26646.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014188. Acrylyl-CoA_reductase_AcuI.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF13. PTHR11695:SF13. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02823. oxido_YhdH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase."
    Li S.-J., Cronan J.E. Jr.
    J. Biol. Chem. 267:855-863(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and resembles yhdH of E. coli and other bacteria in conferring resistance to acrylate."
    Todd J.D., Curson A.R., Sullivan M.J., Kirkwood M., Johnston A.W.
    PLoS ONE 7:E35947-E35947(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    Strain: K12 / BW25113.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry nameiACUI_ECOLI
AccessioniPrimary (citable) accession number: P26646
Secondary accession number(s): Q2M8W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The zinc-binding residues of the alcohol dehydrogenase family are not conserved.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.