GUAA_USTMA
ID GUAA_USTMA Reviewed; 543 AA.
AC Q4P763; A0A0D1DUS8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=GUA1; ORFNames=UMAG_04050;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; CM003150; KIS68009.1; -; Genomic_DNA.
DR RefSeq; XP_011390491.1; XM_011392189.1.
DR AlphaFoldDB; Q4P763; -.
DR SMR; Q4P763; -.
DR STRING; 5270.UM04050P0; -.
DR EnsemblFungi; KIS68009; KIS68009; UMAG_04050.
DR GeneID; 23564338; -.
DR KEGG; uma:UMAG_04050; -.
DR VEuPathDB; FungiDB:UMAG_04050; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; Q4P763; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 392369at2759; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000561; Chromosome 11.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Cytoplasm; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..543
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000286155"
FT DOMAIN 11..204
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 205..418
FT /note="GMPS ATP-PPase"
FT ACT_SITE 87
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 233..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 543 AA; 60291 MW; 7421D2938981321A CRC64;
MTEAIHSQYD SILILDFGSQ YSHLITRRCR ELNVYCEMLP CTQKIKDLDW KPKGIILSGS
PYSVYDEVAP RVDPDVFTAG VPVLGICYGL QEIAWNHGGK VDPHDKREYG HAMVEVVKHG
VPHLDALFKN WEGSVQVWMS HGDQLSKAPE DFVVIAKTPT APFAAMAHKS KPIYGVQFHP
EVTHSLRGVE LFDSFVDICA CRRDWTMETF IDKEIKRIRE IVGPKGQVLG AISGGVDSSV
AAKLMHEAIG DRFHAVMVDN GVLRTNEAAQ VYEMLSKDLG VNLTVVDASE QFLSRLKDVE
DPEQKRKIIG NTFIHVFEAE VAKLEKQAED EEAAALAAGK PQEAKGKFEY LLQGTLYPDV
IESISFKGPS ATIKTHHNVG GLLEDMKLKL IEPLRELFKD EVRALGKLLG IPAHLVGRHP
FPGPGLAIRI LGPVTREQVK ILQHADSIYI DEIRAAGLYD QISQAFAVLL PVRAVGVQGD
KRTYDQVIAL RAAATTDFMT ATWYPFPAEF LSKVSNRITN EVQGVNRVVL DISSKPPATI
EWL
