GUAA_BIFLO
ID GUAA_BIFLO Reviewed; 535 AA.
AC Q8G5P4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BL0960;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN24772.1; -; Genomic_DNA.
DR RefSeq; NP_696136.1; NC_004307.2.
DR AlphaFoldDB; Q8G5P4; -.
DR SMR; Q8G5P4; -.
DR STRING; 206672.BL0960; -.
DR MEROPS; C26.957; -.
DR PRIDE; Q8G5P4; -.
DR EnsemblBacteria; AAN24772; AAN24772; BL0960.
DR KEGG; blo:BL0960; -.
DR PATRIC; fig|206672.9.peg.664; -.
DR HOGENOM; CLU_014340_0_5_11; -.
DR OMA; KRKIIGH; -.
DR PhylomeDB; Q8G5P4; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000439; 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..535
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140097"
FT DOMAIN 20..210
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 211..409
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 184
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 186
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 238..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 535 AA; 57866 MW; 252A91136E3EE8A0 CRC64;
MFSPRKIPMN VRGISMANGP VLVVDFGAQY AQLIARRVRE AGVYSELVPH SMPVDEILAK
DPKAIILSGG PASVFEPGAP TIDTKVFESG VPVLGICYGF QVMAYELGGK VDKAALGEYG
KTSATIDDAA GILADSPAEQ TTWMSHGVAV EQAPAGFEVL AHTEGAPVAA MADESRKLYG
VQWHPEVKHS PLGQKLIENF LHRCAALPND WDASSIIEDQ VKKIREQVGD AEVICGLSGG
VDSAVAAALV HKAIGDQLTC VFVDHGLLRK GEVEQVKHDF VAATGIRLIT VDAADDFLDA
LAGVSEPERK RKIIGEKFIR TFEKAQRQVL EEAGARGKEV KFLVQGTLYP DVVESGGGDG
AANIKSHHNV GGLPKDIKFQ LIEPLRTLFK DEVRAIGTEL GLPDEIVWRQ PFPGPGLGIR
IIGEITKERL DLLREADAIA REELSKAGLD RDIWQCPVVL LADVHSVGVQ GDERTYGSPI
VLRPVSSEDA MTADWSRVPY DVLATISTRI TNECRQINRV VLDCTSKPPA TIEWE
