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Protein

Lactaldehyde reductase

Gene

fucO

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

Functioni

Catalytic activityi

(R)-propane-1,2-diol + NAD+ = (R)-lactaldehyde + NADH.
(S)-propane-1,2-diol + NAD+ = (S)-lactaldehyde + NADH.

Cofactori

Fe cation1 Publication

Enzyme regulationi

Inhibited by Zn2+.1 Publication

Pathwayi: L-fucose degradation

This protein is involved in the pathway L-fucose degradation, which is part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the pathway L-fucose degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381NAD
Binding sitei70 – 701NAD
Binding sitei150 – 1501NAD
Binding sitei161 – 1611NAD
Metal bindingi195 – 1951Iron
Metal bindingi199 – 1991Iron; via tele nitrogen
Metal bindingi262 – 2621Iron; via tele nitrogen
Metal bindingi276 – 2761Iron; via tele nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 982NAD
Nucleotide bindingi139 – 1435NAD
Nucleotide bindingi180 – 1845NAD

GO - Molecular functioni

  • ferrous iron binding Source: EcoCyc
  • lactaldehyde reductase activity Source: EcoCyc

GO - Biological processi

  • glycol catabolic process Source: EcoCyc
  • L-fucose catabolic process Source: EcoCyc
  • propanediol metabolic process Source: EcoCyc
  • rhamnose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Keywords - Ligandi

Iron, Metal-binding, NAD

Enzyme and pathway databases

BioCyciEcoCyc:LACTALDREDUCT-MONOMER.
ECOL316407:JW2770-MONOMER.
MetaCyc:LACTALDREDUCT-MONOMER.
UniPathwayiUPA00563.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactaldehyde reductase (EC:1.1.1.77)
Alternative name(s):
Propanediol oxidoreductase
Gene namesi
Name:fucO
Ordered Locus Names:b2799, JW2770
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10351. fucO.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 99MANRMILNE → M: Loss of enzyme activity, loss of dimerization. 1 Publication
Mutagenesisi16 – 161G → D: No effect on enzyme activity. 1 Publication
Mutagenesisi38 – 381D → G: Enzyme can now use NADP. 1 Publication
Mutagenesisi96 – 961G → E: Loss of NAD binding and enzyme activity. 1 Publication
Mutagenesisi195 – 1951D → L: Complete loss of iron-binding. 1 Publication
Mutagenesisi199 – 1991H → A or F: Complete loss of iron-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Lactaldehyde reductasePRO_0000087824Add
BLAST

Proteomic databases

PaxDbiP0A9S1.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259223. 91 interactions.
DIPiDIP-48076N.
IntActiP0A9S1. 5 interactions.
MINTiMINT-1223334.
STRINGi511145.b2799.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi9 – 146Combined sources
Helixi17 – 204Combined sources
Helixi21 – 288Combined sources
Beta strandi32 – 387Combined sources
Helixi39 – 435Combined sources
Helixi46 – 5611Combined sources
Beta strandi60 – 678Combined sources
Helixi73 – 8513Combined sources
Beta strandi89 – 968Combined sources
Helixi97 – 11115Combined sources
Helixi113 – 1153Combined sources
Helixi119 – 1213Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi140 – 1423Combined sources
Turni145 – 1473Combined sources
Beta strandi149 – 1557Combined sources
Turni156 – 1594Combined sources
Beta strandi160 – 1656Combined sources
Helixi167 – 1693Combined sources
Beta strandi172 – 1765Combined sources
Helixi178 – 1803Combined sources
Turni181 – 1833Combined sources
Helixi186 – 20520Combined sources
Helixi211 – 23222Combined sources
Helixi236 – 25621Combined sources
Helixi260 – 27213Combined sources
Helixi276 – 29116Combined sources
Helixi292 – 2943Combined sources
Helixi298 – 3058Combined sources
Helixi315 – 33319Combined sources
Helixi339 – 3424Combined sources
Helixi346 – 3483Combined sources
Helixi349 – 35810Combined sources
Helixi360 – 3645Combined sources
Beta strandi365 – 3673Combined sources
Helixi371 – 38212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRMX-ray1.60A/B1-382[»]
2BI4X-ray2.85A/B1-382[»]
2BL4X-ray2.85A/B1-382[»]
5BR4X-ray0.91A/B1-382[»]
ProteinModelPortaliP0A9S1.
SMRiP0A9S1. Positions 1-382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9S1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C0A. Bacteria.
COG1454. LUCA.
HOGENOMiHOG000243333.
InParanoidiP0A9S1.
KOiK00048.
OMAiDIVGLYQ.

Family and domain databases

InterProiIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR013460. Lactal_redase.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02638. lactal_redase. 1 hit.
PROSITEiPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9S1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANRMILNET AWFGRGAVGA LTDEVKRRGY QKALIVTDKT LVQCGVVAKV
60 70 80 90 100
TDKMDAAGLA WAIYDGVVPN PTITVVKEGL GVFQNSGADY LIAIGGGSPQ
110 120 130 140 150
DTCKAIGIIS NNPEFADVRS LEGLSPTNKP SVPILAIPTT AGTAAEVTIN
160 170 180 190 200
YVITDEEKRR KFVCVDPHDI PQVAFIDADM MDGMPPALKA ATGVDALTHA
210 220 230 240 250
IEGYITRGAW ALTDALHIKA IEIIAGALRG SVAGDKDAGE EMALGQYVAG
260 270 280 290 300
MGFSNVGLGL VHGMAHPLGA FYNTPHGVAN AILLPHVMRY NADFTGEKYR
310 320 330 340 350
DIARVMGVKV EGMSLEEARN AAVEAVFALN RDVGIPPHLR DVGVRKEDIP
360 370 380
ALAQAALDDV CTGGNPREAT LEDIVELYHT AW
Length:382
Mass (Da):40,513
Last modified:November 16, 2011 - v2
Checksum:iE4D927AC8142098B
GO

Sequence cautioni

The sequence AAA23824.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA23825.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB40449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE76871.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA33124.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731N → T in CAA33124 (PubMed:2664711).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31059 Genomic DNA. Translation: AAA23824.1. Different initiation.
X15025 Genomic DNA. Translation: CAA33124.1. Different initiation.
M27177 Genomic DNA. Translation: AAA23825.1. Different initiation.
U29581 Genomic DNA. Translation: AAB40449.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75841.2.
AP009048 Genomic DNA. Translation: BAE76871.1. Different initiation.
L07763 Genomic DNA. No translation available.
PIRiA32883. RDECLA.
RefSeqiNP_417279.2. NC_000913.3.
WP_000013588.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75841; AAC75841; b2799.
BAE76871; BAE76871; BAE76871.
GeneIDi947273.
KEGGiecj:JW2770.
eco:b2799.
PATRICi32121014. VBIEscCol129921_2899.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31059 Genomic DNA. Translation: AAA23824.1. Different initiation.
X15025 Genomic DNA. Translation: CAA33124.1. Different initiation.
M27177 Genomic DNA. Translation: AAA23825.1. Different initiation.
U29581 Genomic DNA. Translation: AAB40449.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75841.2.
AP009048 Genomic DNA. Translation: BAE76871.1. Different initiation.
L07763 Genomic DNA. No translation available.
PIRiA32883. RDECLA.
RefSeqiNP_417279.2. NC_000913.3.
WP_000013588.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRMX-ray1.60A/B1-382[»]
2BI4X-ray2.85A/B1-382[»]
2BL4X-ray2.85A/B1-382[»]
5BR4X-ray0.91A/B1-382[»]
ProteinModelPortaliP0A9S1.
SMRiP0A9S1. Positions 1-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259223. 91 interactions.
DIPiDIP-48076N.
IntActiP0A9S1. 5 interactions.
MINTiMINT-1223334.
STRINGi511145.b2799.

Proteomic databases

PaxDbiP0A9S1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75841; AAC75841; b2799.
BAE76871; BAE76871; BAE76871.
GeneIDi947273.
KEGGiecj:JW2770.
eco:b2799.
PATRICi32121014. VBIEscCol129921_2899.

Organism-specific databases

EchoBASEiEB0347.
EcoGeneiEG10351. fucO.

Phylogenomic databases

eggNOGiENOG4105C0A. Bacteria.
COG1454. LUCA.
HOGENOMiHOG000243333.
InParanoidiP0A9S1.
KOiK00048.
OMAiDIVGLYQ.

Enzyme and pathway databases

UniPathwayiUPA00563.
BioCyciEcoCyc:LACTALDREDUCT-MONOMER.
ECOL316407:JW2770-MONOMER.
MetaCyc:LACTALDREDUCT-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9S1.
PROiP0A9S1.

Family and domain databases

InterProiIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR013460. Lactal_redase.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02638. lactal_redase. 1 hit.
PROSITEiPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol."
    Chen Y.M., Lu Z., Lin E.C.C.
    J. Bacteriol. 171:6097-6105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
    Lu Z., Lin E.C.C.
    Nucleic Acids Res. 17:4883-4884(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae."
    Conway T., Ingram L.O.
    J. Bacteriol. 171:3754-3759(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Sequencing and characterization of the sdaB gene from Escherichia coli K-12."
    Shao Z., Newman E.B.
    Eur. J. Biochem. 212:777-784(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-382.
    Strain: K12.
  7. "Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli."
    Montella C., Bellsolell L., Perez-Luque R., Badia J., Baldoma L., Coll M., Aguilar J.
    J. Bacteriol. 187:4957-4966(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH NAD(+), COFACTOR, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF 1-MET--ASN-9; GLY-16; ASP-38; GLY-96; ASP-195 AND HIS-199.
    Strain: K12 / ECL1.
  8. "Crystal structure of lactaldehyde reductase."
    New York structural genomix research consortium (NYSGXRC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiFUCO_ECOLI
AccessioniPrimary (citable) accession number: P0A9S1
Secondary accession number(s): P11549, Q2MA35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 16, 2011
Last modified: April 13, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.