GUAA_MYCTU
ID GUAA_MYCTU Reviewed; 525 AA.
AC P9WMS7; L0TCE7; P0A5A1; Q50729;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv3396c; ORFNames=MTCY78.32;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22119138; DOI=10.1016/j.abb.2011.11.013;
RA Franco T.M., Rostirolla D.C., Ducati R.G., Lorenzini D.M., Basso L.A.,
RA Santos D.S.;
RT "Biochemical characterization of recombinant guaA-encoded guanosine
RT monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv
RT strain.";
RL Arch. Biochem. Biophys. 517:1-11(2012).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC {ECO:0000269|PubMed:22119138}.
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:22119138};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.24 mM for glutamine {ECO:0000269|PubMed:22119138};
CC KM=27 uM for ATP {ECO:0000269|PubMed:22119138};
CC Vmax=2.49 umol/min/mg enzyme toward XMP (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:22119138};
CC Vmax=2.58 umol/min/mg enzyme toward ATP (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:22119138};
CC Vmax=3.30 umol/min/mg enzyme toward glutamine (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:22119138};
CC Note=kcat is 2.3 sec(-1) for XMP. kcat is 2.39 sec(-1) for ATP. kcat
CC is 3.05 sec(-1) for glutamine.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:22119138};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:22119138};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22119138}.
CC -!- MASS SPECTROMETRY: Mass=55928; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:22119138};
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DR EMBL; AL123456; CCP46218.1; -; Genomic_DNA.
DR PIR; A70735; A70735.
DR RefSeq; NP_217913.1; NC_000962.3.
DR RefSeq; WP_003417952.1; NZ_NVQJ01000027.1.
DR AlphaFoldDB; P9WMS7; -.
DR SMR; P9WMS7; -.
DR STRING; 83332.Rv3396c; -.
DR MEROPS; C26.A07; -.
DR iPTMnet; P9WMS7; -.
DR PaxDb; P9WMS7; -.
DR DNASU; 887412; -.
DR GeneID; 45427392; -.
DR GeneID; 887412; -.
DR KEGG; mtu:Rv3396c; -.
DR PATRIC; fig|83332.111.peg.3785; -.
DR TubercuList; Rv3396c; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR OMA; KRKIIGH; -.
DR PhylomeDB; P9WMS7; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Acetylation; ATP-binding; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140149"
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"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:21969609"
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
