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ECOLI:KDSA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) kdsA
Protein Name(s) 2-dehydro-3-deoxyphosphooctonate aldolase

3-deoxy-D-manno-octulosonic acid 8-phosphate synthase KDO-8-phosphate synthase KDO 8-P synthase KDOPS Phospho-2-dehydro-3-deoxyoctonate aldolase

External Links
UniProt P0A715
EMBL X05552
U18555
U00096
AP009048
PIR I83573
RefSeq NP_415733.1
YP_489482.1
PDB 1D9E
1G7U
1G7V
1GG0
1PHQ
1PHW
1PL9
1Q3N
1X6U
1X8F
PDBsum 1D9E
1G7U
1G7V
1GG0
1PHQ
1PHW
1PL9
1Q3N
1X6U
1X8F
ProteinModelPortal P0A715
SMR P0A715
DIP DIP-35940N
IntAct P0A715
MINT MINT-1220797
STRING 511145.b1215
SWISS-2DPAGE P0A715
PaxDb P0A715
PRIDE P0A715
EnsemblBacteria AAC74299
BAA36073
GeneID 12931123
945785
KEGG ecj:Y75_p1187
eco:b1215
PATRIC 32117682
EchoBASE EB0513
EcoGene EG10518
eggNOG COG2877
HOGENOM HOG000023021
InParanoid P0A715
KO K01627
OMA ESRDHAF
OrthoDB EOG680X4R
PhylomeDB P0A715
BioCyc EcoCyc:KDO-8PSYNTH-MONOMER
ECOL316407:JW1206-MONOMER
MetaCyc:KDO-8PSYNTH-MONOMER
SABIO-RK P0A715
UniPathway UPA00030
UPA00357
EvolutionaryTrace P0A715
PRO PR:P0A715
Proteomes UP000000318
UP000000625
Genevestigator P0A715
GO GO:0005829
GO:0008676
GO:0019294
Gene3D 3.20.20.70
HAMAP MF_00056
InterPro IPR013785
IPR006218
IPR006269
PANTHER PTHR21057:SF2
Pfam PF00793
TIGRFAMs TIGR01362

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:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:10734095[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019294

keto-3-deoxy-D-manno-octulosonic acid biosynthetic process

PMID:8223657[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008676

3-deoxy-8-phosphooctulonate synthase activity

PMID:8223657[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013785

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006269

C

Seeded From UniProt

complete

enables

GO:0008676

3-deoxy-8-phosphooctulonate synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006269

F

Seeded From UniProt

complete

involved_in

GO:0009058

biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006218

P

Seeded From UniProt

complete

enables

GO:0008676

3-deoxy-8-phosphooctulonate synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.5.1.55

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:UR000038406

C

Seeded From UniProt

complete

enables

GO:0008676

3-deoxy-8-phosphooctulonate synthase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038406

F

Seeded From UniProt

complete

involved_in

GO:0009103

lipopolysaccharide biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038406

P

Seeded From UniProt

complete

involved_in

GO:0019294

keto-3-deoxy-D-manno-octulosonic acid biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000038406

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0009103

lipopolysaccharide biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0448
UniPathway:UPA00030

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

Notes

References

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

  1. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. Radaev, S et al. (2000) Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase. J. Biol. Chem. 275 9476-84 PubMed GONUTS page
  3. 3.0 3.1 Baasov, T et al. (1993) Catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase. The use of synthetic analogues to probe the structure of the putative reaction intermediate. Eur. J. Biochem. 217 991-9 PubMed GONUTS page
  4. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  5. 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