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ECOLI:RHMA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) rhmA (synonyms: yfaU)
Protein Name(s) 2-keto-3-deoxy-L-rhamnonate aldolase

KDR aldolase 2-dehydro-3-deoxyrhamnonate aldolase 2-keto-3-deoxy acid sugar aldolase

External Links
UniProt P76469
EMBL U00096
AP009048
PIR C64995
RefSeq NP_416748.1
YP_490484.1
PDB 2VWS
2VWT
PDBsum 2VWS
2VWT
ProteinModelPortal P76469
SMR P76469
DIP DIP-11953N
STRING 511145.b2245
EnsemblBacteria AAC75305
BAA16064
GeneID 12932490
948054
KEGG ecj:Y75_p2208
eco:b2245
PATRIC 32119853
EchoBASE EB3836
EcoGene EG14083
eggNOG COG3836
HOGENOM HOG000179750
InParanoid P76469
KO K12660
OMA IEGAMRT
OrthoDB EOG6NPM5P
PhylomeDB P76469
BioCyc EcoCyc:G7158-MONOMER
ECOL316407:JW2239-MONOMER
MetaCyc:G7158-MONOMER
EvolutionaryTrace P76469
PRO PR:P76469
Proteomes UP000000318
UP000000625
Genevestigator P76469
GO GO:0005737
GO:0016832
GO:0000287
GO:0016151
GO:0006725
Gene3D 3.20.20.60
HAMAP MF_01290
InterPro IPR005000
IPR023593
IPR015813
Pfam PF03328
SUPFAM SSF51621

Annotations

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

enables

GO:0016832

aldehyde-lyase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14083
PANTHER:PTN000766732

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10016
EcoGene:EG14083
PANTHER:PTN000766732

C

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

PMID:18754683[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016151

nickel cation binding

PMID:18754683[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006725

cellular aromatic compound metabolic process

PMID:18754683[2]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q47098

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:18754683[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

PMID:18754683[2]

ECO:0000314

direct assay evidence used in manual assertion

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:IPR005000
InterPro:IPR015813

F

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023593

F

Seeded From UniProt

complete

enables

GO:0106099

2-keto-3-deoxy-L-rhamnonate aldolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.2.53

F

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:UR000101691

F

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101691

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: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

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. 2.0 2.1 2.2 2.3 2.4 Rea, D et al. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 9955-65 PubMed GONUTS page