ID F9WCE4_TRYCI Unreviewed; 657 AA.
AC F9WCE4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=TCIL3000_0_55050 {ECO:0000313|EMBL:CCD14937.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD14937.1, ECO:0000313|Proteomes:UP000000702};
RN [1] {ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702};
RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., Aslett M.,
RA Brown R., Corton N., Harris D., Hauser H., Gamble J., Gilderthorp R.,
RA McQuillan J., Quail M.A., Sanders M., Van Tonder A., Ginger M.L.,
RA Donelson J.E., Field M.C., Barry J.D., Berriman M., Hertz-Fowler C.;
RT "Divergent evolution of antigenic variation in African trypanosomes.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD14937.1, ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD14937.1,
RC ECO:0000313|Proteomes:UP000000702};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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:CCD14937.1}.
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; CAEQ01001707; CCD14937.1; -; Genomic_DNA.
DR AlphaFoldDB; F9WCE4; -.
DR MEROPS; C26.A21; -.
DR VEuPathDB; TriTrypDB:TcIL3000_0_55050; -.
DR OMA; DQLTCMF; -.
DR OrthoDB; 6206at2759; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000702; 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; -; 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:UP000000702}.
FT DOMAIN 201..417
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 229..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 657 AA; 72068 MW; 5CABDD9043A18E76 CRC64;
MSVQPQSEEY IAILDAGSQY GKVIDRRVRE LRVESRVMPL NTPTEVLRGD PSIKGVIISG
GPSSIYDSNA PSYNKDLFEL GKPLLGICYG MQLLTEAFGG EVGRADVRED GQDEITVDTT
SPIFAGLSQR ETVLLTHGDS IISPGTELKV MARSSANIIA AVQHQTRPLF GVQFHPEVEL
TKNGVQILRN FLELCGCAFA FTMEDREEKA LRLIRERTAK GQKVLCLASG GVDSTVCAVL
LLKAIGPERV VCVHIDHGFM RLNESELVVA ALKAAGVNVT LVSAAEQFAQ ATTEFPARRG
KGPYQTGKLC ETKDPEEKRV IIGNTFMAVC NKVVKDLGLD MDNLLLAQGT LRPDLIESGS
LYASKLADAI KTHHNDTDVV RQLREKGQII EPLCDYHKDE VRELGVRLGI PSHLVQRQPF
PGPGLAIRLL CSDGTPFRDK QFAPTEEILR SVCSGDNQFE LLKPLRPTIK NLQPAGCVLP
VRTVGVQGDG RTYAYAAALS LGHFPLGEEW KVLNQLALII PKISTDINRI VFMFGSKRVE
SPKTVTKSFL VPETLNKLRL ADNLVNEVLL KYNLVRRLSQ VAVILLPVGL EEKGDFSIVI
RTFITNDFMT GVPAVPGTPD MPLEALKEMV AALETLDFAS RVMYDMTGKP PGTTEWE
//