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RHORT:Q2RSQ7

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Species (Taxon ID) Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). (269796)
Gene Name(s) glnE (ECO:0000256 with HAMAP-Rule:MF_00802)
Protein Name(s) Glutamate-ammonia-ligase adenylyltransferase (ECO:0000256 with HAMAP-Rule:MF_00802, ECO:0000256 with SAAS:SAAS00048967)

Glutamine-synthase adenylyltransferase (ECO:0000256 with HAMAP-Rule:MF_00802) [Glutamate--ammonia-ligase] adenylyltransferase (ECO:0000256 with HAMAP-Rule:MF_00802)

External Links
UniProt Q2RSQ7
EMBL CP000230
RefSeq YP_427125.1
ProteinModelPortal Q2RSQ7
STRING 269796.Rru_A2038
EnsemblBacteria ABC22838
GeneID 3835464
KEGG rru:Rru_A2038
PATRIC 23327758
eggNOG COG1225
HOGENOM HOG000256492
KO K00982
OMA ENECIEL
OrthoDB EOG651SRZ
BioCyc RRUB269796:GCN1-2072-MONOMER
Proteomes UP000001929
GO GO:0008882
GO:0005524
GO:0016874
GO:0051920
Gene3D 3.40.30.10
HAMAP MF_00802
InterPro IPR000866
IPR023057
IPR005190
IPR013546
IPR012336
Pfam PF00578
PF08335
PF03710
SUPFAM SSF52833
PROSITE PS51352

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051920

peroxiredoxin activity

PMID:17951375[1]

ECO:0000314

F

Figure 3 shows peroxidase activities of the GlnE.

complete
CACAO 3380

GO:0006542

glutamine biosynthetic process

PMID:19761831[2]

ECO:0000315

P

See Figure 1. Summation of three GS activity in three different cultures.

complete
CACAO 3401

involved_in

GO:0006542

glutamine biosynthetic process

PMID:19761831[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051920

peroxiredoxin activity

PMID:17951375[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005623

cell

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0045454

C

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0016209

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0051920

P

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005190
InterPro:IPR023057

F

Seeded From UniProt

complete

enables

GO:0016209

antioxidant activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000866

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000866

F

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013546

F

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013766

P

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:IPR000866

P

Seeded From UniProt

complete

enables

GO:0047388

[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.89

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.42

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0548

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

involved_in

GO:0000820

regulation of glutamine family amino acid metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

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:UR000100229

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Jonsson, A et al. (2008) A novel peroxiredoxin activity is located within the C-terminal end of Rhodospirillum rubrum adenylyltransferase. J. Bacteriol. 190 434-7 PubMed GONUTS page
  2. 2.0 2.1 Jonsson, A et al. (2009) Reduced activity of glutamine synthetase in Rhodospirillum rubrum mutants lacking the adenylyltransferase GlnE. Res. Microbiol. 160 581-4 PubMed GONUTS page