GUAA_MICLC
ID GUAA_MICLC Reviewed; 539 AA.
AC C5CBZ4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Mlut_16470;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
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; CP001628; ACS31135.1; -; Genomic_DNA.
DR RefSeq; WP_012751030.1; NZ_WBMF01000033.1.
DR AlphaFoldDB; C5CBZ4; -.
DR SMR; C5CBZ4; -.
DR STRING; 465515.Mlut_16470; -.
DR MEROPS; C26.A07; -.
DR PRIDE; C5CBZ4; -.
DR EnsemblBacteria; ACS31135; ACS31135; Mlut_16470.
DR KEGG; mlu:Mlut_16470; -.
DR PATRIC; fig|465515.4.peg.1583; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_11; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000738; 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..539
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000205306"
FT DOMAIN 20..211
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 212..413
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 185
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 187
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 239..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 539 AA; 57843 MW; F6EE896CAF32C14F CRC64;
MTQNAPHPDT PAPLSDVMPT VLVLDFGAQY AQLIARRVRE ANVYSEVVPA STPAAQILER
EPAALILSGG PSSVYEPGAP QLDPALLEAG VPVLGLCYGF QSIAHALGGT VAQTGTREYG
STRLDSVDAD SVLFADQDLE QVVWMSHGDA VTQAPEGFAV TASTAGAPVA AFEDRERRIY
GVQWHPEVGH SSRGQRVLEQ FLHEGAGLGA DWTASGVIEE QVERIREQIG DKRAICGLSG
GVDSAVAAAL VQRAIGDRLT CVYVDHGLMR EGESAEIEQA FGEAHGGARL VMVDAREDFL
SALAGVTDPE AKRKIIGERF IRTFEKAQAD IVLESEHDPD ATEVRFLVQG TLYPDVVESG
GGDGAANIKS HHNVGGLPDD IEFELCEPLR ELFKDEVRAV GAELGLPEGI VHRQPFPGPG
LGIRIIGEVT QERLDLLRRA DAIVRAELTA AGLDRQIWQC PVVLLADVRS VGVQGDGRTY
GHPVVLRPVT SEDAMTADWA RIPDDVLSRI SNRITNEVDG VNRVVLDVTS KPPGTIEWE
