GUAA_CLOPE
ID GUAA_CLOPE Reviewed; 509 AA.
AC Q8XI46; Q8RLC2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=CPE2275;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-509.
RC STRAIN=ATCC 3626 / NCIB 10691 / Type B;
RX PubMed=12142405; DOI=10.1128/jb.184.16.4359-4368.2002;
RA Zimmer M., Scherer S., Loessner M.J.;
RT "Genomic analysis of Clostridium perfringens bacteriophage phi3626, which
RT integrates into guaA and possibly affects sporulation.";
RL J. Bacteriol. 184:4359-4368(2002).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC Rule:MF_00344}.
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:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR EMBL; BA000016; BAB81981.1; -; Genomic_DNA.
DR EMBL; AY082069; AAL96770.1; -; Genomic_DNA.
DR RefSeq; WP_003460104.1; NC_003366.1.
DR AlphaFoldDB; Q8XI46; -.
DR SMR; Q8XI46; -.
DR STRING; 195102.gene:10491583; -.
DR EnsemblBacteria; BAB81981; BAB81981; BAB81981.
DR GeneID; 29570332; -.
DR KEGG; cpe:CPE2275; -.
DR HOGENOM; CLU_014340_0_5_9; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
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 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 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..509
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140114"
FT DOMAIN 4..194
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 195..384
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 168
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 222..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 509 AA; 56843 MW; BAA75E1207DB029A CRC64;
MRDLVLVVDF GGQYNQLIAR RVRECGVYCE IIPYTYSIEK IKEKNPKGII FTGGPNSVYG
ENTPTLDKEI FNLNVPVLGI CYGDQLMAHL LGGKVDTAPV REYGKTNVTL DNSSKLFAGI
EADETCWMSH TDYIAEAPEG FKIIAHTDVC PVAAMENEER RLYGVQFHPE VEHTPFGQNM
MRNFLYNICG LENSWSMASF AEEKIAEIKK IVGDKKLICA LSGGVDSSVA AVMVHKAVGK
QLTCIFVDHG LLRKDEGDQV EKIFKEGFDM NLIRVNAQDR FLGKLKGVSD PETKRKIIGE
EFIRVFEEEA GKLGDIKFLV QGTIYPDVVE SGTDTSAVIK SHHNVGGLPE DMEFSLIEPL
RELFKDEVRA VGEELGIPHH LVWRQPFPGP GLAIRVLGEV TEDKLEVVRE ADAIFREEIA
LAGLESEIWQ YFAVLPNIQS VGVMGDERTY CHTVGLRAVT SSDGMTSNWA HIPYEVIDKV
SRRIVNEVKG VNRIVYDVTS KPPATIEWE
