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ECOLI:ULAG

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ulaG (synonyms: yjfR)
Protein Name(s) Probable L-ascorbate-6-phosphate lactonase UlaG

L-ascorbate utilization protein G

External Links
UniProt P39300
EMBL U14003
U00096
AP009048
RefSeq NP_418613.2
YP_492334.1
PDB 2WYL
2WYM
PDBsum 2WYL
2WYM
ProteinModelPortal P39300
SMR P39300
DIP DIP-12596N
STRING 511145.b4192
PRIDE P39300
EnsemblBacteria AAC77149
BAE78193
GeneID 12933718
948705
KEGG ecj:Y75_p4078
eco:b4192
PATRIC 32123959
EchoBASE EB2385
EcoGene EG12492
eggNOG COG2220
HOGENOM HOG000127385
InParanoid P39300
KO K03476
OMA CIVMKPG
OrthoDB EOG696C0T
PhylomeDB P39300
BioCyc EcoCyc:G7855-MONOMER
ECOL316407:JW5868-MONOMER
MetaCyc:G7855-MONOMER
BRENDA 3.1.4.1
UniPathway UPA00263
EvolutionaryTrace P39300
PRO PR:P39300
Proteomes UP000000318
UP000000625
Genevestigator P39300
GO GO:0005737
GO:0035460
GO:0030145
GO:0019854
Gene3D 3.60.15.10
HAMAP MF_01266
InterPro IPR001279
IPR023951
SMART SM00849
SUPFAM SSF56281

Annotations

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

enables

GO:0035460

L-ascorbate 6-phosphate lactonase activity

PMID:20359483[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:20359483[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

PMID:12644495[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023951

P

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023951

F

Seeded From UniProt

complete

enables

GO:0035460

L-ascorbate 6-phosphate lactonase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023951

F

Seeded From UniProt

complete

enables

GO:0052689

carboxylic ester hydrolase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101591

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101591

C

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101591

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00263

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Garces, F et al. (2010) Molecular architecture of the Mn2+-dependent lactonase UlaG reveals an RNase-like metallo-beta-lactamase fold and a novel quaternary structure. J. Mol. Biol. 398 715-29 PubMed GONUTS page
  2. Zhang, Z et al. (2003) The ascorbate transporter of Escherichia coli. J. Bacteriol. 185 2243-50 PubMed GONUTS page