GUAA_CHLPN
ID GUAA_CHLPN Reviewed; 429 AA.
AC Q9Z913;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Putative GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=CPn_0171, CP_0599, CpB0173;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- CAUTION: Could be the product of a pseudogene. Contains an internal
CC deletion relative to its orthologs. {ECO:0000305}.
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DR EMBL; AE001363; AAD18324.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38415.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98381.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98106.1; -; Genomic_DNA.
DR PIR; B72109; B72109.
DR PIR; C86512; C86512.
DR RefSeq; NP_224379.1; NC_000922.1.
DR RefSeq; WP_010882821.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z913; -.
DR SMR; Q9Z913; -.
DR STRING; 115711.CP_0599; -.
DR MEROPS; C26.A21; -.
DR PRIDE; Q9Z913; -.
DR EnsemblBacteria; AAD18324; AAD18324; CPn_0171.
DR EnsemblBacteria; AAF38415; AAF38415; CP_0599.
DR GeneID; 45050218; -.
DR KEGG; cpa:CP_0599; -.
DR KEGG; cpj:guaA; -.
DR KEGG; cpn:CPn_0171; -.
DR KEGG; cpt:CpB0173; -.
DR PATRIC; fig|115713.3.peg.195; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_0; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 5: Uncertain;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..429
FT /note="Putative GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140110"
FT DOMAIN 10..118
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 119..304
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 429 AA; 48243 MW; DBFD3C681109BFEC CRC64;
MQSARRHLNT IFILDFGSQY TYVLAKQVRK LFVYCEVLPW NISVQCLKER APLGIILSGG
PHSVYENKAP HLDPEIYKLG IPILAICYGM QLMARDFGGT VSPGVGEFGY TPIHLYPCEL
FKHIVDCESL DTEIRMSHRD HVTTIPEGFN VIASTSQCSI SGIENTKQRL YGLQFHPEVS
DSTPTGNKIL ETFVQEICSA PTLWNPLYIQ QDLVSKIQDT VIEVFDEVAQ SLDVQWLAQG
TIYSDVIESS RSGHASEVIK SHHNVGGLPK NLKLKLVEPL RYLFKDEVRI LGEALGLSSY
LLDRHPFPGP GLTIRVIGEI LPEYLAILRR ADLIFIEELR KAKLYDKISQ AFALFLPIKS
VSVKGDCRSY GYTIALRAVE STDFMTGRWA YLPCDVLSSC SSRIINEIPE VSRVVYDISD
KPPATIEWE
