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P0A9S2 (FUCO_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactaldehyde reductase

EC=1.1.1.77
Alternative name(s):
Propanediol oxidoreductase
Gene names
Name:fucO
Ordered Locus Names:Z4116, ECs3659
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

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

Cofactor

Iron By similarity.

Pathway

Carbohydrate degradation; L-fucose degradation.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Sequence caution

The sequence AAG57913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB37082.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fucose metabolism
   LigandIron
Metal-binding
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfucose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionlactaldehyde reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Lactaldehyde reductase
PRO_0000087825

Regions

Nucleotide binding97 – 982NAD By similarity
Nucleotide binding139 – 1435NAD By similarity
Nucleotide binding180 – 1845NAD By similarity

Sites

Metal binding1951Iron By similarity
Metal binding1991Iron; via tele nitrogen By similarity
Metal binding2621Iron; via tele nitrogen By similarity
Metal binding2761Iron; via tele nitrogen By similarity
Binding site381NAD By similarity
Binding site701NAD By similarity
Binding site1501NAD By similarity
Binding site1611NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9S2 [UniParc].

Last modified November 16, 2011. Version 2.
Checksum: E4D927AC8142098B

FASTA38240,513
        10         20         30         40         50         60 
MANRMILNET AWFGRGAVGA LTDEVKRRGY QKALIVTDKT LVQCGVVAKV TDKMDAAGLA 

        70         80         90        100        110        120 
WAIYDGVVPN PTITVVKEGL GVFQNSGADY LIAIGGGSPQ DTCKAIGIIS NNPEFADVRS 

       130        140        150        160        170        180 
LEGLSPTNKP SVPILAIPTT AGTAAEVTIN YVITDEEKRR KFVCVDPHDI PQVAFIDADM 

       190        200        210        220        230        240 
MDGMPPALKA ATGVDALTHA IEGYITRGAW ALTDALHIKA IEIIAGALRG SVAGDKDAGE 

       250        260        270        280        290        300 
EMALGQYVAG MGFSNVGLGL VHGMAHPLGA FYNTPHGVAN AILLPHVMRY NADFTGEKYR 

       310        320        330        340        350        360 
DIARVMGVKV EGMSLEEARN AAVEAVFALN RDVGIPPHLR DVGVRKEDIP ALAQAALDDV 

       370        380 
CTGGNPREAT LEDIVELYHT AW 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57913.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB37082.1. Different initiation.
PIRC91086.
E85931.
RefSeqNP_289354.1. NC_002655.2.
NP_311686.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9S2.
SMRP0A9S2. Positions 1-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4116.

Protocols and materials databases

DNASU958299.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57913; AAG57913; Z4116.
BAB37082; BAB37082; BAB37082.
GeneID916534.
958299.
KEGGece:Z4116.
ecs:ECs3659.
PATRIC18356797. VBIEscCol44059_3581.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1454.
HOGENOMHOG000243333.
KOK00048.
OMADIVGLYQ.
OrthoDBEOG6TFCQS.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3623-MONOMER.
UniPathwayUPA00563.

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR013460. Lactal_redase.
[Graphical view]
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
TIGRFAMsTIGR02638. lactal_redase. 1 hit.
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUCO_ECO57
AccessionPrimary (citable) accession number: P0A9S2
Secondary accession number(s): P11549
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 16, 2011
Last modified: May 14, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways