GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:PROA

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) proA (ECO:0000255 with HAMAP-Rule:MF_00412)
Protein Name(s) Gamma-glutamyl phosphate reductase (ECO:0000255 with HAMAP-Rule:MF_00412)

GPR (ECO:0000255 with HAMAP-Rule:MF_00412) Glutamate-5-semialdehyde dehydrogenase (ECO:0000255 with HAMAP-Rule:MF_00412) Glutamyl-gamma-semialdehyde dehydrogenase (ECO:0000255 with HAMAP-Rule:MF_00412) GSA dehydrogenase (ECO:0000255 with HAMAP-Rule:MF_00412)

External Links
UniProt P07004
EMBL X00786
U70214
U00096
AP009048
Z12832
PIR D64749
RefSeq NP_414778.1
YP_488538.1
ProteinModelPortal P07004
SMR P07004
DIP DIP-10568N
IntAct P07004
MINT MINT-1261639
STRING 511145.b0243
SWISS-2DPAGE P07004
PaxDb P07004
PRIDE P07004
EnsemblBacteria AAC73347
BAA77912
GeneID 12930774
946680
KEGG ecj:Y75_p0234
eco:b0243
PATRIC 32115601
EchoBASE EB0760
EcoGene EG10767
eggNOG COG0014
HOGENOM HOG000246356
InParanoid P07004
KO K00147
OMA CNAIETL
OrthoDB EOG6FFSCX
PhylomeDB P07004
BioCyc EcoCyc:GLUTSEMIALDEHYDROG-MONOMER
ECOL316407:JW0233-MONOMER
MetaCyc:GLUTSEMIALDEHYDROG-MONOMER
UniPathway UPA00098
PRO PR:P07004
Proteomes UP000000318
UP000000625
Genevestigator P07004
GO GO:0005737
GO:0004350
GO:0050661
GO:0055129
GO:0006561
Gene3D 3.40.309.10
3.40.605.10
HAMAP MF_00412
InterPro IPR016161
IPR016163
IPR016162
IPR015590
IPR000965
IPR020593
IPR012134
Pfam PF00171
PIRSF PIRSF000151
SUPFAM SSF53720
TIGRFAMs TIGR00407
PROSITE PS01223

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0047443

4-hydroxy-4-methyl-2-oxoglutarate aldolase activity

PMID:11826967[1]

ECO:0000314

F

Figure 5 (B) shows a strain (containing the gene proA) grown in the presence of IPTG showing the same expression level as a purified strain of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from P. ochraceae.

complete
CACAO 4091

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10767
PANTHER:PTN000115463
SGD:S000005850
UniProtKB:P54886

F

Seeded From UniProt

complete

involved_in

GO:0055129

L-proline biosynthetic process

PMID:791096[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:7035170[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

PMID:7035170[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

PMID:7034716[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

PMID:6337636[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

PMID:6319365[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000965
InterPro:IPR012134
InterPro:IPR020593

F

Seeded From UniProt

complete

involved_in

GO:0006561

proline biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000965
InterPro:IPR012134
InterPro:IPR020593

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015590
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163

F

Seeded From UniProt

complete

enables

GO:0016620

oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016163

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012134

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:IPR000965
InterPro:IPR012134
InterPro:IPR015590
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR020593

P

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.1.41

F

Seeded From UniProt

complete

enables

GO:0004350

glutamate-5-semialdehyde dehydrogenase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001295

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:UR000001295

C

Seeded From UniProt

complete

involved_in

GO:0006561

proline biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001295

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:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

involved_in

GO:0006561

proline biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0641

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

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:0055129

L-proline biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00098

P

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ Maruyama, K et al. (2001) Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem. 65 2701-9 PubMed GONUTS page
  2. ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ Inuzuka, M et al. (1976) Specific action of 4-nitropyridine 1-oxide on Excherichia coli K-12 pro+ strains leading to the isolation of proline-requiring mutants: isolation and characterization of pro-mutants. Antimicrob. Agents Chemother. 10 325-32 PubMed GONUTS page
  4. ↑ 4.0 4.1 Hayzer, DJ & Leisinger, T (1982) Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase. Eur. J. Biochem. 121 561-5 PubMed GONUTS page
  5. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. ↑ 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
  7. ↑ Hayzer, DJ & Leisinger, T (1981) Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase. Biochem. J. 197 269-74 PubMed GONUTS page
  8. ↑ Hayzer, DJ & Leisinger, T (1983) Proline biosynthesis in Escherichia coli. Kinetic and mechanistic properties of glutamate semialdehyde dehydrogenase. Biochim. Biophys. Acta 742 391-8 PubMed GONUTS page
  9. ↑ Smith, CJ et al. (1984) Purification and characteristics of a gamma-glutamyl kinase involved in Escherichia coli proline biosynthesis. J. Bacteriol. 157 545-51 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=ECOLI:PROA&oldid=5953530"