ID A3PK79_RHOS1 Unreviewed; 518 AA. AC A3PK79; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 22-JUL-2008, entry version 11. DE SubName: Full=GMP synthase (Glutamine-hydrolyzing); DE EC=6.3.5.2; GN OrderedLocusNames=Rsph17029_1635; OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P., Mackenzie C., Choudhary M., RA Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC RT 17029."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 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 CC (glutamine route): step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Contains 1 GMP-binding domain. 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; CP000577; ABN76745.1; -; Genomic_DNA. DR RefSeq; YP_001043517.1; -. DR GeneID; 4895146; -. DR GenomeReviews; CP000577_GR; Rsph17029_1635. DR KEGG; rsh:Rsph17029_1635; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-...; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR011702; GATASE. DR InterPro; IPR012998; GATase_1_AS. DR InterPro; IPR000991; GATase_class1_C. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; TrmU_MeTrfase. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF03054; tRNA_Me_trans; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00096; GATASE. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS00442; GATASE_TYPE_I; 1. PE 3: Inferred from homology; KW Complete proteome; GMP biosynthesis; Glutamine amidotransferase; KW Ligase; Purine biosynthesis. SQ SEQUENCE 518 AA; 56985 MW; 2AC907AD076C11C1 CRC64; MTQHDRLLII DFGSQVTQLI ARRLRELNVY CEIHPYQNVT EAFLKGFAPK AVIFSGGPSS VFAEGAPMPP AGVFDLGVPI LGICYGQQVM MHCLGGKVER GHGTAEFGRA FVTPTAERLA ILDGWFEEGR EQVWMSHGDH VSQIAPGFQV FGTSPNAPFA ITGDPARHFY AVQFHPEVHH TPKGAKLYEN FVRLAGFKGD WTMGAYREEA IARIRAQVGD QKVICGLSGG VDSSVAAVLI HEAIGDQLTC VFVDHGLLRL GEAEQVVTMF RDHYNMPLIH ADESDLFLGA LEGVSDPEVK RKTIGRLFID VFQKHAADVG GATFLAQGTL YPDVIESVSF SGGPSVTIKS HHNVGGLPEK MGLKLVEPLR ELFKDEVRAL GRELGLPESF IGRHPFPGPG LAIRCPGEIT REKLEILRRA DAVYIDQIRR HGLYDEIWQA FVALLPVRTV GVMGDGRTYD YACALRAVTS VDGMTADYYP FTHDFLGETA TRIINEVQGI NRVTYDITSK PPGTIEWE //