ID A0A016RYN9_9BILA Unreviewed; 680 AA.
AC A0A016RYN9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Name=Acey_s0343.g3057 {ECO:0000313|EMBL:EYB83079.1};
GN Synonyms=Acey-M106.4 {ECO:0000313|EMBL:EYB83079.1};
GN ORFNames=Y032_0343g3057 {ECO:0000313|EMBL:EYB83079.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB83079.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB83079.1}.
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DR EMBL; JARK01001679; EYB83079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016RYN9; -.
DR STRING; 53326.A0A016RYN9; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR Gene3D; 3.30.300.10; -; 1.
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; 1.
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:UP000024635}.
FT DOMAIN 248..457
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 275..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 680 AA; 75103 MW; 60023AEB435120F4 CRC64;
MRAKRASIEV WKSGVSRTDR LPPPHKRLNS DHLGTQRLEK MGINGKNDEH TDIERVAVLD
FGAQYGKVID RRVREANLLS EMFPLKAKAK DILSKGKFKA IIISGGPNSV YAKGAPQLDE
EIFTCGLPVL GICYGFQLLN KGHGGGVAKE QVREDGQCSV RLDTSCELFH GLNESEQVLL
THGDSVTEAT VAPGFKVVAT SGGHVAGIAC AEKRLYGVQF HPEVDLTING RKIFDNFLFR
IAGCSGGYTL SNREQMCIDE IRQTVGEKKA LVLVSGGVDS SVCAALLNRA LGPQRVTAIH
IDNGFMRKDE SDHVVKSLKA IDLPVHREYA GLMFMVGTVS GKHGDSEPLD RTVDPEIKRQ
IIGNTFIRVK DRVMDELKLK KEDYFLAQGT LRPDLIESAS ELASGHADTI KTHHNDTALV
RELRASGRVI EPLKDFHKDE VRELGRSLGL PDELVDRQPF PGPGLAIRII CAQKPHICSD
FGTTHQCLNV LTNLSRQPTT PFEEEYREKM LAAMSGWEIS ELLSQSFAIY STLLPIKSVG
VQGDSRSYSY VAALSSAQTP IPWQLLARYA TVIPKLLHNI NRVVYVFGDP VVYPVTTITP
TYLNAFTVKT LQEADHVATE ALHGRRVDGS RDPNLVDLSK KVQQFLLLGS LFVEGITAYP
VFENCLSSGC HHRCEKIWFS
//
