GUAA_MYCLE
ID GUAA_MYCLE Reviewed; 529 AA.
AC P46810; Q9CCU9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=ML0395; ORFNames=B1620_C2_205;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC43222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00015; AAC43222.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583918; CAC29903.1; -; Genomic_DNA.
DR PIR; C86958; C86958.
DR PIR; S72813; S72813.
DR RefSeq; NP_301383.1; NC_002677.1.
DR RefSeq; WP_010907707.1; NC_002677.1.
DR AlphaFoldDB; P46810; -.
DR SMR; P46810; -.
DR STRING; 272631.ML0395; -.
DR MEROPS; C26.A07; -.
DR EnsemblBacteria; CAC29903; CAC29903; CAC29903.
DR KEGG; mle:ML0395; -.
DR PATRIC; fig|272631.5.peg.667; -.
DR Leproma; ML0395; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_11; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000806; 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..529
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140146"
FT DOMAIN 16..205
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 206..403
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 529 AA; 56723 MW; 443EDE9525CDD949 CRC64;
MADSAGLDQP EPSPRPVLVV DFGAQYAQLI ARRVREARVF SEVIPHTTSI EEITARDPLA
IVLSGGPASV YTEGAPQLDP ALFDLGLPVF GICYGFQAMA QVLGGTVART KTSEYGRTEL
KVLGGDLHSG LPGVQPVWMS HGDAVTAAPD GFDVAASSSG APVAAFENRD RRLAGVQYHP
EVMHTPHGQQ VLSRFLHDFA GLDADWTAAN IAGVLVEQVR AQIGNGHAIC GLSGGVDSAV
AAALVQRAIG DRLTCIFVDH GLLRDGERGQ VQRDFVAATG AKLVTVDAAE TFLQALSGVT
NPEGKRKIIG RQFIRAFEGA VRDLLGDSTF DSGIEFLVQG TLYPDVVESG GGSGTANIKS
HHNVGGLPDN LRFKLVEPLR LLFKDEVRAV GRQLDLPEEI VARQPFPGPG LGIRIVGEVT
AERLDTLRRA DSIAREELTT AGLDYQIWQC PVVLLADVRS VGVQGDNRSY GHPIVLRPVS
SEDAMTADWT WVPYEVLECI STRITNEVAE VNRVVLDITN KPPGTIEWE
