ID A7SNA7_NEMVE Unreviewed; 701 AA.
AC A7SNA7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN ORFNames=NEMVEDRAFT_v1g191624 {ECO:0000313|EMBL:EDO34799.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO34799.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO34799.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR EMBL; DS469718; EDO34799.1; -; Genomic_DNA.
DR RefSeq; XP_001626899.1; XM_001626849.1.
DR AlphaFoldDB; A7SNA7; -.
DR STRING; 45351.A7SNA7; -.
DR EnsemblMetazoa; EDO34799; EDO34799; NEMVEDRAFT_v1g191624.
DR GeneID; 5506184; -.
DR KEGG; nve:5506184; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_2_1; -.
DR InParanoid; A7SNA7; -.
DR OMA; IWQSFAV; -.
DR OrthoDB; 6206at2759; -.
DR PhylomeDB; A7SNA7; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; 3.30.300.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 225..443
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 252..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 701 AA; 77019 MW; 05124278AB537624 CRC64;
MAANLSKSSA MGSCMNGHIT RDDSSMSELP QNHERVVILD AGAQYGKVID RRVRELNVES
DVLPLDTSIS TIQEKGYKAI IISGGPNSVY AEDALKYDPA LFTIGIPILG ICYGLQMMNK
EFGGSVVKKD SREDGVFNIT VKPSSALFRG LDPHQEVLLT HGDSLDRVAT GFKIIAQSGD
IVAAIENESR KLYGVQFHPE VDLSVNGLAM LKNFLYGVAG CCGTYTVGSR LHTCLREIRH
TVGNHKVLVL VSGGVDSTVC AALLHKALGP DRVVAVHIDN GFMRKQESMQ VEESLKCLGL
RLKVLNAGFQ FYNGSTVISG RKDQIAVKKQ LTKTLNQVSD PEEKRKIIGD TFMKVANDVV
KELELDPNLT FLAQGTLRPD LIESASHIAS GQADAIKTHH NDTELVRVLR EKGRVVEPLK
DFHKDEVRQL GLELGLPTDI VHRHPFPGPG LAIRILCGEE PYQENDFADT NIILGQIVDY
AAAVVKPHSL FVRVRNSTND EEKERLLIIT SKYKIAASLL PIKSVGVQGD GRSYSYVVAL
SSNDKPDWES LMYLARVIPK VCHNINRVCY AFGKRIKFQI QDITTTYLTL GVLSQLRQAD
HVAHSTLSEH GCAGNVSQMP IVSIPVHFDR DPIDHIPSCQ RSIVIRTFIT NDFMTGIPAT
PGKHIPVQVV EGIVAAIQKV QGVSRVLYDL TSKPPGTTEW E
//
