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ECOLI:FUCO

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fucO
Protein Name(s) Lactaldehyde reductase

Propanediol oxidoreductase

External Links
UniProt P0A9S1
EMBL M31059
X15025
M27177
U29581
U00096
AP009048
L07763
PIR A32883
RefSeq NP_417279.2
YP_491007.1
PDB 1RRM
2BI4
2BL4
PDBsum 1RRM
2BI4
2BL4
ProteinModelPortal P0A9S1
SMR P0A9S1
DIP DIP-48076N
IntAct P0A9S1
MINT MINT-1223334
STRING 511145.b2799
PaxDb P0A9S1
EnsemblBacteria AAC75841
BAE76871
GeneID 12930229
947273
KEGG ecj:Y75_p2736
eco:b2799
PATRIC 32121014
EchoBASE EB0347
EcoGene EG10351
eggNOG COG1454
HOGENOM HOG000243333
InParanoid P0A9S1
KO K00048
OMA DIVGLYQ
BioCyc EcoCyc:LACTALDREDUCT-MONOMER
ECOL316407:JW2770-MONOMER
MetaCyc:LACTALDREDUCT-MONOMER
UniPathway UPA00563
EvolutionaryTrace P0A9S1
PRO PR:P0A9S1
Proteomes UP000000318
UP000000625
Genevestigator P0A9S1
GO GO:0008198
GO:0008912
GO:0042846
GO:0042355
GO:0051143
GO:0019301
InterPro IPR001670
IPR018211
IPR013460
Pfam PF00465
TIGRFAMs TIGR02638
PROSITE PS00913
PS00060

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005829

cytosol

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10351
PANTHER:PTN002608693

C

Seeded From UniProt

complete

enables

GO:0004022

alcohol dehydrogenase (NAD) activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12293
EcoGene:EG14183
PANTHER:PTN002608572
PomBase:SPAC5H10.06c
SGD:S000003225

F

Seeded From UniProt

complete

involved_in

GO:0051143

propanediol metabolic process

PMID:15995211[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042846

glycol catabolic process

PMID:9851711[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042355

L-fucose catabolic process

PMID:17709419[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019301

rhamnose catabolic process

PMID:7016842[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008912

lactaldehyde reductase activity

PMID:40956[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:9851711[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001670
InterPro:IPR018211

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001670
InterPro:IPR018211

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001670
InterPro:IPR018211

P

Seeded From UniProt

complete

enables

GO:0008912

lactaldehyde reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.77

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0006004

fucose metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0294

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0019317

fucose catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00563

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Montella, C et al. (2005) Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli. J. Bacteriol. 187 4957-66 PubMed GONUTS page
  3. 3.0 3.1 Obradors, N et al. (1998) Site-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli. Eur. J. Biochem. 258 207-13 PubMed GONUTS page
  4. Autieri, SM et al. (2007) L-fucose stimulates utilization of D-ribose by Escherichia coli MG1655 DeltafucAO and E. coli Nissle 1917 DeltafucAO mutants in the mouse intestine and in M9 minimal medium. Infect. Immun. 75 5465-75 PubMed GONUTS page
  5. Boronat, A & Aguilar, J (1981) Metabolism of L-fucose and L-rhamnose in Escherichia coli: differences in induction of propanediol oxidoreductase. J. Bacteriol. 147 181-5 PubMed GONUTS page
  6. Boronat, A & Aguilar, J (1979) Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. J. Bacteriol. 140 320-6 PubMed GONUTS page
  7. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page