ID F0QR95_MYCSL Unreviewed; 538 AA.
AC F0QR95;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN Name=guaA {ECO:0000313|EMBL:ADX98015.1};
GN OrderedLocusNames=MSU_0479 {ECO:0000313|EMBL:ADX98015.1};
OS Mycoplasma suis (strain Illinois).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=768700 {ECO:0000313|EMBL:ADX98015.1, ECO:0000313|Proteomes:UP000007484};
RN [1] {ECO:0000313|EMBL:ADX98015.1, ECO:0000313|Proteomes:UP000007484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Illinois {ECO:0000313|EMBL:ADX98015.1,
RC ECO:0000313|Proteomes:UP000007484};
RX PubMed=21317328; DOI=10.1128/JB.00133-11;
RA Messick J.B., Santos A.P., Guimaraes A.M.;
RT "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL J. Bacteriol. 193:2068-2069(2011).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC {ECO:0000256|ARBA:ARBA00002332}.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR EMBL; CP002525; ADX98015.1; -; Genomic_DNA.
DR RefSeq; WP_013609114.1; NC_015155.1.
DR AlphaFoldDB; F0QR95; -.
DR STRING; 768700.MSU_0479; -.
DR KEGG; mss:MSU_0479; -.
DR HOGENOM; CLU_014340_0_5_14; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000007484; 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-UniRule.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADX98015.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000007484}.
FT DOMAIN 218..413
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT COILED 210..241
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 245..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 538 AA; 61340 MW; A0103B326382A56A CRC64;
MSVNLSSKRE NKVLFIDLGS QYSCVLERKL KSLGCNITKY FFEEEKVPPE EFTFSNFGVV
FLSGSPASVS EVDDKAGYSW LKNEIISSKQ VPIMGICFGM QLIHHFFGGK IEQVDPLFGE
SQIERERNHP LFLNIPQKFK IWGSFNESVT KLGHGFYSLA NRGKISMISS HVTRSIYTIQ
FHPELNETEF GDQLFRNFLV EISNVELEEN NKEIDNSREI NSKIEALREK YKEQLKDARI
LVALSGGLDS SVLIHFLAEM TIDRNIYPVY ISTGLVPKEK EEKVIKYFAN KFSNFRVVSW
EDSIFNDLKS VTSPEEKRKI IAQKFKKTFD EIYEQEVKRN ITHLAQGTIY SDVIESGKLS
SKYSKIKTHH NVEMVKNESS LPYKVVEPLS DLFKDQVRML GARLNLPAFL LSQQPFPGPG
LAIRVIGEVT KEKVELISSL HDFMEREFIE RKIGKYSDQH FPILLPGQAV GVKGDQRVYG
NAVVLRAVKT IDFMSANVSQ IPLSELVSLA NKMVSKFPQV SRVLFDLTTK PGGTIEWE
//
