Lactaldehyde reductase - Escherichia coli (strain K12)

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P0A9S1 (FUCO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lactaldehyde reductase
EC=1.1.1.77

Alternative name(s):
Propanediol oxidoreductase

Gene names

Name:	fucO
Ordered Locus Names:	b2799, JW2770

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.7
Enzyme regulation	Inhibited by Zn²⁺. Ref.7
Pathway	Carbohydrate degradation; L-fucose degradation.
Subunit structure	Homodimer. Ref.7
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.
Sequence caution	The sequence AAA23824.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAA23825.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAB40449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAE76871.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA33124.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Ligand	Iron Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-fucose catabolic process Inferred from mutant phenotype. Source: EcoCyc glycol catabolic process Inferred from direct assay. Source: EcoCyc propanediol metabolic process Inferred from direct assay Ref.7. Source: EcoCyc rhamnose catabolic process Inferred from expression pattern. Source: EcoCyc
Molecular function	ferrous iron binding Inferred from direct assay. Source: EcoCyc lactaldehyde reductase activity Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Lactaldehyde reductase

PRO_0000087824

Regions

Nucleotide binding

97 – 98

NAD

Nucleotide binding

139 – 143

NAD

Nucleotide binding

180 – 184

NAD

Sites

Metal binding

195

Iron

Metal binding

199

Iron; via tele nitrogen

Metal binding

262

Iron; via tele nitrogen

Metal binding

276

Iron; via tele nitrogen

Binding site

NAD

Binding site

NAD

Binding site

150

NAD

Binding site

161

NAD

Experimental info

Mutagenesis

1 – 9

MANRMILNE → M: Loss of enyzme activity, loss of dimerization. Ref.7

Mutagenesis

G → D: No effect on enzyme activity. Ref.7

Mutagenesis

D → G: Enzyme can now use NADP. Ref.7

Mutagenesis

G → E: Loss of NAD binding and enzyme activity. Ref.7

Mutagenesis

195

D → L: Complete loss of iron-binding. Ref.7

Mutagenesis

199

H → A or F: Complete loss of iron-binding. Ref.7

Sequence conflict

273

N → T in CAA33124. Ref.2

Secondary structure

382

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9S1 [UniParc].

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

FASTA

382

40,513

        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

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2553671] [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: 2664711] [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: 2661535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 8385012] [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: 15995211] [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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

RDECLA. A32883.

RefSeq

NP_417279.2. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RRM	X-ray	1.60	A/B	1-382	[»]
2BI4	X-ray	2.85	A/B	1-382	[»]
2BL4	X-ray	2.85	A/B	1-382	[»]

ProteinModelPortal

P0A9S1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48076N.

IntAct

P0A9S1. 4 interactions.

MINT

MINT-1223334.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003861; EBESCP00000003861; EBESCG00000003156.
EBESCT00000015747; EBESCP00000015038; EBESCG00000014807.

GeneID

947273.

GenomeReviews

Gene locus JW2770 in contig AP009048_GR.
Gene locus b2799 in contig U00096_GR.

KEGG

ecj:JW2770.
eco:b2799.

PATRIC

32121014. VBIEscCol129921_2899.

Organism-specific databases

EchoBASE

EB0347.

EcoGene

EG10351. fucO.

Phylogenomic databases

eggNOG

COG1454.

GeneTree

EBGT00050000009177.

HOGENOM

HBG742415.

OMA

ALNDVCT.

PhylomeDB

P0A9S1.

ProtClustDB

PRK10624.

Enzyme and pathway databases

BioCyc

EcoCyc:LACTALDREDUCT-MONOMER.
MetaCyc:LACTALDREDUCT-MONOMER.

Gene expression databases

Genevestigator

P0A9S1.

Family and domain databases

InterPro

IPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR013460. Lactal_redase.
[Graphical view]

K00048.

Pfam

PF00465. Fe-ADH. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02638. Lactal_redase. 1 hit.

PROSITE

PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FUCO_ECOLI

Accession

Primary (citable) accession number: P0A9S1
Secondary accession number(s): P11549, Q2MA35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	November 16, 2011
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents