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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)DescriptionActionsGraphical viewLength
Binding sitei41NADP; via amide nitrogen1 Publication1
Binding sitei198NADP1 Publication1
Binding sitei242NADP; via amide nitrogen1 Publication1
Binding sitei256NADP; via carbonyl oxygen1 Publication1
Binding sitei267NADP1 Publication1
Binding sitei313NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 159NADP1 Publication4
Nucleotide bindingi178 – 180NADP1 Publication3

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.
MetaCyc:EG11315-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001694931 – 324Probable acrylyl-CoA reductase AcuIAdd BLAST324

Proteomic databases

EPDiP26646.
PaxDbiP26646.
PRIDEiP26646.

2D gel databases

SWISS-2DPAGEP26646.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi14 – 19Combined sources6
Helixi22 – 24Combined sources3
Beta strandi29 – 38Combined sources10
Helixi41 – 48Combined sources8
Helixi50 – 52Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi63 – 72Combined sources10
Beta strandi82 – 86Combined sources5
Turni88 – 92Combined sources5
Beta strandi97 – 104Combined sources8
Helixi106 – 108Combined sources3
Helixi118 – 140Combined sources23
Helixi145 – 147Combined sources3
Beta strandi149 – 154Combined sources6
Helixi158 – 169Combined sources12
Beta strandi174 – 179Combined sources6
Helixi181 – 183Combined sources3
Helixi184 – 190Combined sources7
Beta strandi192 – 197Combined sources6
Helixi198 – 200Combined sources3
Beta strandi201 – 203Combined sources3
Beta strandi212 – 219Combined sources8
Helixi221 – 229Combined sources9
Beta strandi231 – 239Combined sources9
Beta strandi246 – 252Combined sources7
Helixi253 – 258Combined sources6
Beta strandi261 – 264Combined sources4
Beta strandi267 – 269Combined sources3
Helixi272 – 285Combined sources14
Helixi288 – 291Combined sources4
Beta strandi296 – 298Combined sources3
Helixi300 – 302Combined sources3
Helixi303 – 311Combined sources9
Beta strandi319 – 322Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26646.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D3Z. Bacteria.
COG0604. LUCA.
HOGENOMiHOG000294662.
InParanoidiP26646.
KOiK19745.
OMAiAQMDYNS.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O89X-ray2.25A2-324[»]
1O8CX-ray2.60A/B/C/D2-324[»]
ProteinModelPortaliP26646.
SMRiP26646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261942. 8 interactors.
DIPiDIP-12295N.
IntActiP26646. 6 interactors.
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.
PhylomeDBiP26646.

Enzyme and pathway databases

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

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: November 2, 2016
This is version 122 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.