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UniProtKB/Swiss-Prot entry P04079


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GUAA_ECOLI
Primary accession number P04079
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 95)
Name and origin of the protein
Protein name GMP synthase [glutamine-hydrolyzing]
Synonyms EC 6.3.5.2
Glutamine amidotransferase
GMP synthetase
GMPS
Gene name
Name: guaA
OrderedLocusNames: b2507, JW2491
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-17.
PubMed=3894345 [NCBI, ExPASy, EBI, Israel, Japan]
Tiedeman A.A., Smith J.M., Zalkin H.;
"Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12.";
J. Biol. Chem. 260:8676-8679(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
DOMAIN GATASE.
PubMed=2982857 [NCBI, ExPASy, EBI, Israel, Japan]
Zalkin H., Argos P., Narayana S.V.L., Tiedeman A.A., Smith J.M.;
"Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.";
J. Biol. Chem. 260:3350-3354(1985).
[6]
REGULATION OF EXPRESSION BY DNAA.
PubMed=1736096 [NCBI, ExPASy, EBI, Israel, Japan]
Tesfa-Selase F., Drabble W.T.;
"Regulation of the gua operon of Escherichia coli by the DnaA protein.";
Mol. Gen. Genet. 231:256-264(1992).
[7]
ENZYME REGULATION.
DOI=10.1021/bi981980r; PubMed=9890911 [NCBI, ExPASy, EBI, Israel, Japan]
Deras M.L., Chittur S.V., Davisson V.J.;
"N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase.";
Biochemistry 38:303-310(1999).
[8]
REGULATION OF EXPRESSION BY CRP.
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948;
DOI=10.1111/j.1574-6968.2000.tb09146.x; PubMed=10856643 [NCBI, ExPASy, EBI, Israel, Japan]
Hutchings M.I., Drabble W.T.;
"Regulation of the divergent guaBA and xseA promoters of Escherichia coli by the cyclic AMP receptor protein.";
FEMS Microbiol. Lett. 187:115-122(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1038/nsb0196-74; PubMed=8548458 [NCBI, ExPASy, EBI, Israel, Japan]
Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L.;
"The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.";
Nat. Struct. Biol. 3:74-86(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M10101; AAB18619.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75560.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24640; SYECGU.
RefSeq AP_003093.1; -.
NP_417002.1; -.
3D structure databases
PDB
1GPM; X-ray; 2.20 A; A/B/C/D=1-525.[ExPASy / RCSB / EBI]
PDBsum 1GPM; -.
ModBase P04079.
Protein-protein interaction databases
DIP DIP:9852N; -.
IntAct P04079; -.
Enzyme and pathway databases
BioCyc EcoCyc:GMP-SYN-MON; -.
MetaCyc:GMP-SYN-MON; -.
Organism-specific databases
EchoBASE EB0415; -.
EcoGene EG10420; guaA.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003922; Molecular function: GMP synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004808; Molecular function: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0009058; Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006541; Biological process: glutamine metabolic process (inferred from electronic annotation from InterPro).
GO:0006177; Biological process: GMP biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008033; Biological process: tRNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00344; -; 1.
PBIL [Tree]
InterPro IPR006220; Anth_synthII.
IPR001317; CarbamoylP_synth_GATase.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
IPR001674; GMP_synth_C.
IPR004739; GMP_synth_N.
IPR014729; Rossmann-like_a/b/a_fold.
IPR004506; TrmU_MeTrfase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF00117; GATase; 1.
PF00958; GMP_synt_C; 1.
PF03054; tRNA_Me_trans; 1.
Pfam graphical view of domain structure.
PRINTS PR00097; ANTSNTHASEII.
PR00099; CPSGATASE.
PR00096; GATASE.
TIGRFAMs TIGR00884; guaA_Cterm; 1.
TIGR00888; guaA_Nterm; 1.
PROSITE PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P04079.
Genome annotation databases
GeneID 947334; -.
GenomeReviews U00096_GR; b2507.
AP009048_GR; JW2491.
KEGG ecj:JW2491; -.
eco:b2507; -.
Phylogenomic databases
HOGENOM P04079; -.
Other
DrugBank DB00131; Adenosine monophosphate.
LinkHub P04079; -.
Genome annotation databases
CMR P04079; b2507.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   525  525     GMP synthase [glutamine-hydrolyzing]. PRO_0000140123
DOMAIN   9   207  199     Glutamine amidotransferase type-1. 
DOMAIN   239   401  163     GMP-binding. 
NP_BIND   235   241  7     ATP. 
ACT_SITE   86    86        Nucleophile. 
ACT_SITE   181   181         
ACT_SITE   183   183         
CONFLICT   3     3        E -> N (in Ref. 1; AA sequence). 
STRAND   7    14  8      
HELIX   20    29  10      
STRAND   33    39  7      
HELIX   43    49  7      
STRAND   52    56  5      
HELIX   73    76  4      
STRAND   78    80  3      
STRAND   82    85  4      
HELIX   87    95  9      
STRAND   99   101  3      
STRAND   107   115  9      
TURN   120   124  5      
STRAND   127   129  3      
STRAND   135   143  9      
STRAND   145   149  5      
STRAND   155   159  5      
STRAND   166   170  5      
TURN   171   174  4      
STRAND   175   180  6      
HELIX   190   199  10      
HELIX   210   225  16      
STRAND   229   233  5      
HELIX   238   251  14      
HELIX   252   254  3      
STRAND   255   261  7      
HELIX   269   277  9      
TURN   278   281  4      
STRAND   285   289  5      
HELIX   291   298  8      
HELIX   304   325  22      
STRAND   326   333  8      
HELIX   338   343  6      
STRAND   371   373  3      
TURN   375   378  4      
HELIX   381   390  10      
HELIX   395   398  4      
HELIX   407   410  4      
HELIX   418   437  20      
HELIX   441   443  3      
STRAND   444   457  14      
TURN   460   462  3      
STRAND   465   479  15      
STRAND   482   485  4      
HELIX   490   503  14      
STRAND   507   513  7      
Sequence information
Length: 525 AA [This is the length of the unprocessed precursor] Molecular weight: 58679 Da [This is the MW of the unprocessed precursor] CRC64: D934786DFF3D694B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN PSGIILSGGP 

        70         80         90        100        110        120 
ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EASNEREFGY AQVEVVNDSA 

       130        140        150        160        170        180 
LVRGIEDALT ADGKPLLDVW MSHGDKVTAI PSDFITVAST ESCPFAIMAN EEKRFYGVQF 

       190        200        210        220        230        240 
HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS 

       250        260        270        280        290        300 
SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG 

       310        320        330        340        350        360 
ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN 

       370        380        390        400        410        420 
VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY 

       430        440        450        460        470        480 
CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF 

       490        500        510        520 
MTAHWAHLPY DFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE 

P04079 in FASTA format

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