ID GUAA_MYCBO Reviewed; 525 AA.
AC P0A5A2; A0A1R3Y480; Q50729; X2BPF9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=BQ2027_MB3429C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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}.
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DR EMBL; LT708304; SIU02058.1; -; Genomic_DNA.
DR RefSeq; NP_857070.1; NC_002945.3.
DR RefSeq; WP_003417952.1; NC_002945.4.
DR AlphaFoldDB; P0A5A2; -.
DR SMR; P0A5A2; -.
DR GeneID; 45427392; -.
DR PATRIC; fig|233413.5.peg.3764; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase 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; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00884; guaA_Cterm; 1.
DR NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 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..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140150"
FT DOMAIN 16..205
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 206..399
FT /note="GMPS ATP-PPase"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT BINDING 233..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 56060 MW; DFBE06100BA16FAF CRC64;
MVQPADIDVP ETPARPVLVV DFGAQYAQLI ARRVREARVF SEVIPHTASI EEIRARQPVA
LVLSGGPASV YADGAPKLDP ALLDLGVPVL GICYGFQAMA QALGGIVAHT GTREYGRTEL
KVLGGKLHSD LPEVQPVWMS HGDAVTAAPD GFDVVASSAG APVAAFEAFD RRLAGVQYHP
EVMHTPHGQQ VLSRFLHDFA GLGAQWTPAN IANALIEQVR TQIGDGHAIC GLSGGVDSAV
AAALVQRAIG DRLTCVFVDH GLLRAGERAQ VQRDFVAATG ANLVTVDAAE TFLEALSGVS
APEGKRKIIG RQFIRAFEGA VRDVLDGKTA EFLVQGTLYP DVVESGGGSG TANIKSHHNV
GGLPDDLKFT LVEPLRLLFK DEVRAVGREL GLPEEIVARQ PFPGPGLGIR IVGEVTAKRL
DTLRHADSIV REELTAAGLD NQIWQCPVVL LADVRSVGVQ GDGRTYGHPI VLRPVSSEDA
MTADWTRVPY EVLERISTRI TNEVAEVNRV VLDITSKPPA TIEWE
//
