ID GUAAA_META3 Reviewed; 188 AA. AC A6UVC9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 21-SEP-2011, entry version 27. DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A; DE EC=6.3.5.2; DE AltName: Full=Glutamine amidotransferase; GN Name=guaAA; OrderedLocusNames=Maeo_0869; OS Methanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=419665; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nankai-3 / ATCC BAA-1280; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus aeolicus Nankai-3."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + xanthosine 5'-phosphate + L-glutamine + CC H(2)O = AMP + diphosphate + GMP + L-glutamate. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase CC subunit (A) and a GMP-binding subunit (B) (Potential). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000743; ABR56451.1; -; Genomic_DNA. DR RefSeq; YP_001325063.1; NC_009635.1. DR ProteinModelPortal; A6UVC9; -. DR STRING; A6UVC9; -. DR GeneID; 5326839; -. DR GenomeReviews; CP000743_GR; Maeo_0869. DR KEGG; mae:Maeo_0869; -. DR eggNOG; arNOG05587; -. DR HOGENOM; HBG292341; -. DR OMA; GQYVHRI; -. DR ProtClustDB; PRK00758; -. DR BioCyc; MAEO419665:MAEO_0869-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_01510; GMP_synthase_A; 1; -. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR011702; GATASE. DR InterPro; IPR017926; GATASE_1. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR023686; GMP_synthase_A. DR Pfam; PF00117; GATase; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00096; GATASE. DR TIGRFAMs; TIGR00888; GuaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis. FT CHAIN 1 188 GMP synthase [glutamine-hydrolyzing] FT subunit A. FT /FTId=PRO_0000316093. FT DOMAIN 1 188 Glutamine amidotransferase type-1. FT ACT_SITE 76 76 Nucleophile (By similarity). FT ACT_SITE 163 163 By similarity. FT ACT_SITE 165 165 By similarity. SQ SEQUENCE 188 AA; 20877 MW; 2540A7E6E98378CC CRC64; MIVILNNGGQ YVHRIHRSLR YLKIPSKIIP NSTPLAEIEE NKEIKGIILS GGPDIEKASN CLDIALNSKL PILGICLGHQ IIAKAYGGEI GRAESEEYAH SKIFVKEEND LFKNVPKEFT AWASHKDEVV GAPLNFEILA YSNICEVEAM KHKEKPIYGV QFHPEVSHTE NGAEILKNFC KVCGLLGE //