Reviewed, UniProtKB/Swiss-Prot P04079 (GUAA_ECOLI)

Names and origin

Protein names

Recommended name:
    GMP synthase [glutamine-hydrolyzing]
    EC=6.3.5.2
Alternative name(s):
    Glutamine amidotransferase
    GMP synthetase
      Short name=GMPS

Gene names

Name:	guaA
Ordered Locus Names:	b2507, JW2491

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the synthesis of GMP from XMP. HAMAP MF_00344
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_00344
Enzyme regulation	Inhibited by 2-fluoroinosine 5'-monophosphate (F-IMP) and by N(2)-hydroxyguanosine 5'-monophosphate (N(2)-OH-GMP). Ref.7
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (glutamine route): step 1/1. HAMAP MF_00344
Subunit structure	Homodimer. HAMAP MF_00344
Induction	Activated by cAMP receptor protein (CRP). Repressed by dnaA. HAMAP MF_00344
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain. Contains 1 GMP-binding domain.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
oppA	P23843	1	EBI-909122,EBI-1123030

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 525

525

GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344

PRO_0000140123

Regions

Domain

9 – 207

199

Glutamine amidotransferase type-1

Domain

239 – 401

163

GMP-binding

Nucleotide binding

235 – 241

7

ATP HAMAP MF_00344

Sites

Active site

86

1

Nucleophile HAMAP MF_00344

Active site

181

1

HAMAP MF_00344

Active site

183

1

HAMAP MF_00344

Experimental info

Sequence conflict

3

1

E → N AA sequence Ref.1

Secondary structure

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525

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Helix

20 – 29

10

Beta strand

33 – 39

7

Helix

43 – 49

7

Beta strand

52 – 56

5

Helix

73 – 76

4

Beta strand

78 – 80

3

Beta strand

82 – 85

4

Helix

87 – 95

9

Beta strand

99 – 101

3

Beta strand

107 – 115

9

Turn

120 – 124

5

Beta strand

127 – 129

3

Beta strand

135 – 143

9

Beta strand

145 – 149

5

Beta strand

155 – 159

5

Beta strand

166 – 170

5

Turn

171 – 174

4

Beta strand

175 – 180

6

Helix

190 – 199

10

Helix

210 – 225

16

Beta strand

229 – 233

5

Helix

238 – 251

14

Helix

252 – 254

3

Beta strand

255 – 261

7

Helix

269 – 277

9

Turn

278 – 281

4

Beta strand

285 – 289

5

Helix

291 – 298

8

Helix

304 – 325

22

Beta strand

326 – 333

8

Helix

338 – 343

6

Beta 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

Beta strand

444 – 457

14

Turn

460 – 462

3

Beta strand

465 – 479

15

Beta strand

482 – 485

4

Helix

490 – 503

14

Beta strand

507 – 513

7

Sequences

	Sequence		Length	Mass (Da)
	P04079-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: D934786DFF3D694B	FASTA	525	58,679
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12." Tiedeman A.A., Smith J.M., Zalkin H. J. Biol. Chem. 260:8676-8679(1985) [PubMed: 3894345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17.
[2]	"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." 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. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase." Zalkin H., Argos P., Narayana S.V.L., Tiedeman A.A., Smith J.M. J. Biol. Chem. 260:3350-3354(1985) [PubMed: 2982857] [Abstract] Cited for: DOMAIN GATASE.
[6]	"Regulation of the gua operon of Escherichia coli by the DnaA protein." Tesfa-Selase F., Drabble W.T. Mol. Gen. Genet. 231:256-264(1992) [PubMed: 1736096] [Abstract] Cited for: REGULATION OF EXPRESSION BY DNAA.
[7]	"N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase." Deras M.L., Chittur S.V., Davisson V.J. Biochemistry 38:303-310(1999) [PubMed: 9890911] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Regulation of the divergent guaBA and xseA promoters of Escherichia coli by the cyclic AMP receptor protein." Hutchings M.I., Drabble W.T. FEMS Microbiol. Lett. 187:115-122(2000) [PubMed: 10856643] [Abstract] Cited for: REGULATION OF EXPRESSION BY CRP. Strain: K12 / JM101 / ATCC 33876 / DSM 3948.
[9]	"The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families." Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L. Nat. Struct. Biol. 3:74-86(1996) [PubMed: 8548458] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M10101 Genomic DNA. Translation: AAB18619.1.
U00096 Genomic DNA. Translation: AAC75560.1.
AP009048 Genomic DNA. Translation: BAA16394.1.

PIR

SYECGU. A24640.

RefSeq

AP_003093.1.
NP_417002.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GPM	X-ray	2.20	A/B/C/D	1-525	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9852N.

IntAct

P04079. 8 interactions.

PTM databases

PhosSite

P04079.

Genome annotation databases

GeneID

947334.

GenomeReviews

Gene locus JW2491 in contig AP009048_GR.
Gene locus b2507 in contig U00096_GR.

KEGG

ecj:JW2491.
eco:b2507.

Organism-specific databases

EchoBASE

EB0415.

EcoGene

EG10420. guaA.

CMR

Search...

Phylogenomic databases

HOGENOM

P04079.

OMA

P04079. NEGDMVM.

Enzyme and pathway databases

BioCyc

EcoCyc:GMP-SYN-MON.
MetaCyc:GMP-SYN-MON.

BRENDA

6.3.4.1. 246.

Family and domain databases

HAMAP

MF_00344.
[Tree]

InterPro

IPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR014729. Rossmann-like_a/b/a_fold.
IPR018318. tRNA_MeTrfase-like.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

Pfam

PF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF03054. tRNA_Me_trans. 1 hit.
[Graphical view]

PRINTS

PR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.

TIGRFAMs

TIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

GUAA_ECOLI

Accession

Primary (citable) accession number: P04079

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)