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guaA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

GuaA

Synonyms

GMP synthetase (glutamine aminotransferase)[1], B2507[2][1], GuaA[2][1]

Product description

GuaA[2]; GMP synthetase[3];

Component of GMP-SYN-CPLX[2]

GMP synthase[4]

EC number (for enzymes)

Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0003922

GMP synthase (glutamine-hydrolyzing) activity

PMID:9890911[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003921

GMP synthase activity

PMID:17103135[7]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc [8]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P23843

F

Seeded from EcoCyc [8]

complete

GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [8]

complete

GO:0003922

GMP synthase (glutamine-hydrolyzing) activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001674
InterPro:IPR004739
EC:6.3.5.2
HAMAP:MF_00344

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0004808

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004506

F

Seeded from EcoCyc [8]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001674
InterPro:IPR004739
SP_KW:KW-0067
HAMAP:MF_00344

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005737

cytoplasm

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004506

C

Seeded from EcoCyc [8]

complete

GO:0006177

GMP biosynthetic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001674
InterPro:IPR004739
SP_KW:KW-0332
HAMAP:MF_00344

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0006541

glutamine metabolic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001317
InterPro:IPR011702
SP_KW:KW-0315

P

Seeded from EcoCyc [8]

complete

GO:0008033

tRNA processing

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004506

P

Seeded from EcoCyc [8]

complete

GO:0006177

GMP biosynthetic process

PMID:4353875[10]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0003824

catalytic activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000991
InterPro:IPR001317
InterPro:IPR006220
InterPro:IPR011702

F

Seeded from EcoCyc [8]

complete

GO:0005829

cytosol

PMID:16858726[11]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [8]

complete

GO:0009058

biosynthetic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006220

P

Seeded from EcoCyc [8]

complete

GO:0016874

ligase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0436

F

Seeded from EcoCyc [8]

complete

GO:0015949

nucleobase, nucleoside and nucleotide interconversion

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0003922

GMP synthase (glutamine-hydrolyzing) activity

PMID:9890911[5]

IDA

F

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006177

GMP biosynthetic process

PMID:4353875[10]

IMP

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0003921

GMP synthase activity

PMID:17103135[7]

IDA

F

Seeded from EcoCyc 11.1[3].

required fields missing

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner TypePartnerNotesReferencesEvidence

Protein

Subunits of GMP-SYN-CPLX

could be indirect

Protein

nadE

PMID:16606699[9]

Experiment(s):EBI-1143063

Protein

phnN

PMID:16606699[9]

Experiment(s):EBI-1143063

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc

MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN PSGIILSGGP
ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EASNEREFGY AQVEVVNDSA
LVRGIEDALT ADGKPLLDVW MSHGDKVTAI PSDFITVAST ESCPFAIMAN EEKRFYGVQF
HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS
SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG
ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN
VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY
CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF
MTAHWAHLPY DFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE
Length

525

Mol. Wt

58.678 kDa

pI

5.2 (calculated)

Extinction coefficient

64,860 - 65,735 (calc based on 14 Y, 8 W, and 7 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

TypeResiduesDescriptionNotesReferences

Modification Site

357

phosphorylation site at S357

probability greater than 75%

PMID:17938405[12]


rectanglemotifs

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures
Models

View models at:

Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource typeSourceNotes/Reference

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:GMP-SYN-MONOMER

UniProt (EcoliWiki Page)

UniProt:P04079

PFAM (EcoliWiki Page)

PFAM:PF00117

RefSeq (EcoliWiki Page)

RefSeq:NP_417002


Notes

Links

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References

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

  1. 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 3.3 3.4 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 Deras ML et al. (1999) N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase. Biochemistry 38: 303-10 PubMed EcoliWiki page
  6. 6.0 6.1 6.2 6.3 6.4 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. 7.0 7.1 Abbott JL et al. (2006) The effects of removing the GAT domain from E. coli GMP synthetase. Protein J 25: 483-91 PubMed EcoliWiki page
  8. 8.00 8.01 8.02 8.03 8.04 8.05 8.06 8.07 8.08 8.09 8.10 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  9. 9.0 9.1 9.2 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  10. 10.0 10.1 Lambden PR & Drabble WT (1973) The gua operon of Escherichia coli K-12: evidence for polarity from guaB to guaA. J Bacteriol 115: 992-1002 PubMed EcoliWiki page
  11. 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 EcoliWiki page
  12. Macek B et al. (2007) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics PubMed EcoliWiki page

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