ID A0A158PQD7_BRUPA Unreviewed; 1028 AA.
AC A0A158PQD7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JAN-2026, entry version 45.
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=BPAG_LOCUS1587 {ECO:0000313|EMBL:VDN82773.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|WBParaSite:BPAG_0000160601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000160601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN82773.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR EMBL; UZAD01000136; VDN82773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PQD7; -.
DR STRING; 6280.A0A158PQD7; -.
DR WBParaSite; BPAG_0000160601-mRNA-1; BPAG_0000160601-mRNA-1; BPAG_0000160601.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000278627; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000008; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.620:FF:000044; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.880:FF:000013; GMP synthase [glutamine-hydrolyzing]; 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 NCBIfam; NF000848; PRK00074.1; 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 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:UP000278627}.
FT DOMAIN 550..758
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT REGION 69..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..110
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..146
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 577..583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 1028 AA; 112994 MW; 64A1189CAA8F7155 CRC64;
MCDLKCICIN RRYGTNSGRL KSKGDVMSIS MSKHSPHNLP CTYTDEYFAA GEQGENVVSS
PRGVHLKLPN TGSSLSSSFD SNNPISLVSD SSRNKSDTLD STKSSDSSSL ARALPNLSKK
HTSILRPFLR KKTKLTSSSG NSPGSGSDHR ETNRNIEGEA MKRTASPTLP GGATRAKYDS
TICNEEIDVS SSFHAVNATT GTDSLKIMKN GISNSPVCDA VECHYRIYVE KWVSKTTGID
TAESCRLTVV IIVGGWDRSS VIALVVLPLI TCVSSTAGVL TVVGSLQERK TIEESSLQRT
VSLNKDSRTL CSTDASVSME VQPVDYTNGK KATDIPNGIT SAVHLNNTKL ENAYKGGVAI
LDFGAQFGKV IDRRVREQNV FSEILPFNTK AADMVEKGCY KAIILSGGPN SVNSFNAPEF
DPSILTCGIP VLGICYGFQL INKAFGGCVS KKSVREDGQL EIEVDTTCPL FKGLATRQKV
LLTHGDSVTD KTVANDFKVV GRSGNFVAAI ADERRKLYGV QFHPEVDLSV SGKKILHNFL
FRIAGVIDGF TIDNREQKCI QEIRSVVVDK KVLVMVSGGV DSTVCAALLH KALGSDRVIA
IHIDNGFMRS NESDQVVDLL NELNLKVRKY SAFYAFMNGR IQIGNELSTP LMGTIQPELK
RKIIGDTFMR VKDKIMDELK LDKDIFLAQG TLRPDLIESA SHLASSHADV IKTHHNDSAL
VRELRDLGKV LEPLKDFHKD EVRELGISLG LPEHVVHRHP FPGPGLAIRI VCAERPLISD
FDLFVTTQHH LHLIANLSLC DKDSEEFSTI TQHLSKADLK IISGHDFEIA TTLLPVQSVG
VQGDGRSYAY VAALSTNERP IPWELLERLA HIIPRLLHNI NRVVYVFGNA VEYPVNDVTR
TYLNGFTVGL VKWADRIASD VLCGLGENGK RDLTLDVCLQ KIQQMPVVMI PIHFDRDPLE
RRASTLRSFV LRPFITNDFM TGVAALPGKD IPEQNILEIV RRIMERIPLT SRIMIDLTSK
PPGTTEWE
//
