GUAA_BACSU
ID GUAA_BACSU Reviewed; 513 AA.
AC P29727; O34531;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 154.
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=BSU06360;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / DE1;
RX PubMed=1312531; DOI=10.1128/jb.174.6.1883-1890.1992;
RA Maentsaelae P., Zalkin H.;
RT "Cloning and sequence of Bacillus subtilis purA and guaA, involved in the
RT conversion of IMP to AMP and GMP.";
RL J. Bacteriol. 174:1883-1890(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 149 AND 459-463.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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; M83691; AAA22497.1; -; Genomic_DNA.
DR EMBL; U51115; AAB62311.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12455.2; -; Genomic_DNA.
DR PIR; C69638; C69638.
DR RefSeq; NP_388517.2; NC_000964.3.
DR RefSeq; WP_003244399.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P29727; -.
DR SMR; P29727; -.
DR IntAct; P29727; 2.
DR MINT; P29727; -.
DR STRING; 224308.BSU06360; -.
DR MEROPS; C26.957; -.
DR jPOST; P29727; -.
DR PRIDE; P29727; -.
DR EnsemblBacteria; CAB12455; CAB12455; BSU_06360.
DR GeneID; 936028; -.
DR KEGG; bsu:BSU06360; -.
DR PATRIC; fig|224308.179.peg.691; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR InParanoid; P29727; -.
DR OMA; KRKIIGH; -.
DR PhylomeDB; P29727; -.
DR BioCyc; BSUB:BSU06360-MON; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..513
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140093"
FT DOMAIN 8..198
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 199..388
FT /note="GMPS ATP-PPase"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT BINDING 227..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="S -> T (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> AA (in Ref. 1; AAA22497 and 2; AAB62311)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="A -> G (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Y -> H (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="C -> S (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="T -> Q (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> G (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> R (in Ref. 1; AAA22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 459..463
FT /note="GIRAV -> ESRR (in Ref. 1; AAA22497 and 2; AAB62311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57849 MW; BBD6426FE37D41BB CRC64;
MTKLVNEMIL VLDFGSQYNQ LITRRIREFG VYSELHPHTL TAEEIKKMNP KGIILSGGPN
SVYDENSFRC DEKIFELDIP VLGICYGMQL MTHYLGGKVE AASQREYGKA NIRIEGTPDL
FRDLPNEQVV WMSHGDLVVE VPEGFTVDAT SHHCPNSAMS KADKKWYGVQ FHPEVRHSEY
GNDLLKNFVF GVCECEGEWS MENFIEIEMQ KIRETVGDKQ VLCALSGGVD SSVVAVLIHK
AIGDQLTCIF VDHGLLRKGE AEGVMKTFSE GFNMNVIKVD AKDRFLNKLK GVSDPEQKRK
IIGNEFIYVF DDEADKLKGI DYLAQGTLYT DIIESGTATA QTIKSHHNVG GLPEDMQFEL
IEPLNTLFKD EVRALGTELG IPDEIVWRQP FPGPGLGIRV LGEVTEEKLE IVRESDAILR
EEIANHGLER DIWQYFTVLP DIRSVGVMGD ARTYDYTIGI RAVTSIDGMT SDWARIPWDV
LEVISTRIVN EVKHINRVVY DITSKPPATI EWE
