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ECOLI:ULAD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ulaD (synonyms: sgaH, yjfV)
Protein Name(s) 3-keto-L-gulonate-6-phosphate decarboxylase UlaD

3-dehydro-L-gulonate-6-phosphate decarboxylase KGPDC L-ascorbate utilization protein D

External Links
UniProt P39304
EMBL U14003
U00096
AP009048
PIR S56421
RefSeq NP_418617.1
YP_492338.1
PDB 1KV8
1KW1
1Q6L
1Q6O
1Q6Q
1Q6R
1SO3
1SO4
1SO5
1SO6
1XBV
1XBX
1XBY
1XBZ
PDBsum 1KV8
1KW1
1Q6L
1Q6O
1Q6Q
1Q6R
1SO3
1SO4
1SO5
1SO6
1XBV
1XBX
1XBY
1XBZ
ProteinModelPortal P39304
SMR P39304
DIP DIP-10869N
IntAct P39304
STRING 511145.b4196
SWISS-2DPAGE P39304
PRIDE P39304
EnsemblBacteria AAC77153
BAE78197
GeneID 12933006
948714
KEGG ecj:Y75_p4082
eco:b4196
PATRIC 32123967
EchoBASE EB2389
EcoGene EG12496
eggNOG COG0269
HOGENOM HOG000226068
InParanoid P39304
KO K03078
OMA TIPTMKA
OrthoDB EOG66B435
PhylomeDB P39304
BioCyc EcoCyc:G7858-MONOMER
ECOL316407:JW4154-MONOMER
MetaCyc:G7858-MONOMER
SABIO-RK P39304
UniPathway UPA00263
EvolutionaryTrace P39304
PRO PR:P39304
Proteomes UP000000318
UP000000625
Genevestigator P39304
GO GO:0033982
GO:0000287
GO:0004590
GO:0006207
GO:0019854
Gene3D 3.20.20.70
HAMAP MF_01267
InterPro IPR023942
IPR013785
IPR001754
IPR011060
Pfam PF00215
SMART SM00934
SUPFAM SSF51366

Annotations

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

enables

GO:0033982

3-dehydro-L-gulonate-6-phosphate decarboxylase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12285
EcoGene:EG12496
PANTHER:PTN002170082

F

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12496
PANTHER:PTN002170082

P

Seeded From UniProt

complete

enables

GO:0033982

3-dehydro-L-gulonate-6-phosphate decarboxylase activity

PMID:11741871[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019854

L-ascorbic acid catabolic process

PMID:14996803[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:11900527[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023942

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011060
InterPro:IPR013785

F

Seeded From UniProt

complete

enables

GO:0004590

orotidine-5'-phosphate decarboxylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001754

F

Seeded From UniProt

complete

involved_in

GO:0006207

'de novo' pyrimidine nucleobase biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001754

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:IPR023942

P

Seeded From UniProt

complete

enables

GO:0033982

3-dehydro-L-gulonate-6-phosphate decarboxylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023942

F

Seeded From UniProt

complete

enables

GO:0033982

3-dehydro-L-gulonate-6-phosphate decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.85

F

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:UR000101594

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101594

F

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101594

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

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0210

F

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

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 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. Yew, WS & Gerlt, JA (2002) Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184 302-6 PubMed GONUTS page
  3. Campos, E et al. (2004) Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in LaAscorbate dissimilation in Escherichia coli. J. Bacteriol. 186 1720-8 PubMed GONUTS page
  4. Wise, E et al. (2002) Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 41 3861-9 PubMed GONUTS page