GUAA_ECOLI
ID GUAA_ECOLI Reviewed; 525 AA.
AC P04079;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2 {ECO:0000269|PubMed:9890911};
DE AltName: Full=GMP synthetase;
DE Short=GMPS;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=b2507, JW2491;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-17.
RX PubMed=3894345; DOI=10.1016/s0021-9258(17)39400-0;
RA Tiedeman A.A., Smith J.M., Zalkin H.;
RT "Nucleotide sequence of the guaA gene encoding GMP synthetase of
RT Escherichia coli K12.";
RL J. Biol. Chem. 260:8676-8679(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP DOMAIN GATASE.
RX PubMed=2982857; DOI=10.1016/s0021-9258(19)83627-x;
RA Zalkin H., Argos P., Narayana S.V.L., Tiedeman A.A., Smith J.M.;
RT "Identification of a trpG-related glutamine amide transfer domain in
RT Escherichia coli GMP synthetase.";
RL J. Biol. Chem. 260:3350-3354(1985).
RN [6]
RP REGULATION OF EXPRESSION BY DNAA.
RX PubMed=1736096; DOI=10.1007/bf00279799;
RA Tesfa-Selase F., Drabble W.T.;
RT "Regulation of the gua operon of Escherichia coli by the DnaA protein.";
RL Mol. Gen. Genet. 231:256-264(1992).
RN [7]
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=9890911; DOI=10.1021/bi981980r;
RA Deras M.L., Chittur S.V., Davisson V.J.;
RT "N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of
RT Escherichia coli guanosine monophosphate synthetase.";
RL Biochemistry 38:303-310(1999).
RN [8]
RP REGULATION OF EXPRESSION BY CRP.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=10856643; DOI=10.1111/j.1574-6968.2000.tb09146.x;
RA Hutchings M.I., Drabble W.T.;
RT "Regulation of the divergent guaBA and xseA promoters of Escherichia coli
RT by the cyclic AMP receptor protein.";
RL FEMS Microbiol. Lett. 187:115-122(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8548458; DOI=10.1038/nsb0196-74;
RA Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L.;
RT "The crystal structure of GMP synthetase reveals a novel catalytic triad
RT and is a structural paradigm for two enzyme families.";
RL Nat. Struct. Biol. 3:74-86(1996).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC Evidence={ECO:0000269|PubMed:9890911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681;
CC Evidence={ECO:0000305|PubMed:9890911};
CC -!- ACTIVITY REGULATION: Inhibited by 2-fluoroinosine 5'-monophosphate (F-
CC IMP) and by N(2)-hydroxyguanosine 5'-monophosphate (N(2)-OH-GMP).
CC {ECO:0000269|PubMed:9890911}.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P04079; P04079: guaA; NbExp=3; IntAct=EBI-909122, EBI-909122;
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP). Repressed by DnaA.
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DR EMBL; M10101; AAB18619.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75560.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16394.1; -; Genomic_DNA.
DR PIR; A24640; SYECGU.
DR RefSeq; NP_417002.1; NC_000913.3.
DR RefSeq; WP_000138270.1; NZ_LN832404.1.
DR PDB; 1GPM; X-ray; 2.20 A; A/B/C/D=1-525.
DR PDBsum; 1GPM; -.
DR AlphaFoldDB; P04079; -.
DR SMR; P04079; -.
DR BioGRID; 4259645; 51.
DR DIP; DIP-9852N; -.
DR IntAct; P04079; 8.
DR STRING; 511145.b2507; -.
DR DrugBank; DB04272; Citric acid.
DR MEROPS; C26.957; -.
DR jPOST; P04079; -.
DR PaxDb; P04079; -.
DR PRIDE; P04079; -.
DR EnsemblBacteria; AAC75560; AAC75560; b2507.
DR EnsemblBacteria; BAA16394; BAA16394; BAA16394.
DR GeneID; 947334; -.
DR KEGG; ecj:JW2491; -.
DR KEGG; eco:b2507; -.
DR PATRIC; fig|1411691.4.peg.4230; -.
DR EchoBASE; EB0415; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_6; -.
DR InParanoid; P04079; -.
DR OMA; KRKIIGH; -.
DR PhylomeDB; P04079; -.
DR BioCyc; EcoCyc:GMP-SYN-MON; -.
DR BioCyc; MetaCyc:GMP-SYN-MON; -.
DR BRENDA; 6.3.5.2; 2026.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; P04079; -.
DR PRO; PR:P04079; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:EcoCyc.
DR GO; GO:0003921; F:GMP synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IMP:EcoCyc.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00344; GMP_synthase; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR022955; GMP_synthase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing;
KW Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140123"
FT DOMAIN 9..207
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 208..400
FT /note="GMPS ATP-PPase"
FT ACT_SITE 86
FT /note="Nucleophile"
FT ACT_SITE 181
FT ACT_SITE 183
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT CONFLICT 3
FT /note="E -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1GPM"
FT TURN 120..124
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1GPM"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:1GPM"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 304..325
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1GPM"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 418..437
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 444..457
FT /evidence="ECO:0007829|PDB:1GPM"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 465..479
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:1GPM"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:1GPM"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:1GPM"
SQ SEQUENCE 525 AA; 58679 MW; D934786DFF3D694B CRC64;
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
