ID T1HLK0_RHOPR Unreviewed; 1063 AA.
AC T1HLK0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC004924-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC004924-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR EMBL; ACPB03008382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HLK0; -.
DR STRING; 13249.T1HLK0; -.
DR EnsemblMetazoa; RPRC004924-RA; RPRC004924-PA; RPRC004924.
DR VEuPathDB; VectorBase:RPRC004924; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_0_0_1; -.
DR InParanoid; T1HLK0; -.
DR OMA; ENAAYYY; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT DOMAIN 519..710
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1063 AA; 118187 MW; 7D41CF6D089B6DBA CRC64;
NKQCILLLED GTSYKGYNFG ASSSINGEVV FQTGMVGYVE SLTDPSYHAQ ILVLTYPLIG
NYGVPSAEND EFNLPKWFES HKIWAAGLVV GEACETPSHW QSNKTLSQWL EANNVPGIAG
IDTRDLTKKI RHKGSILGKI INENFPSPKS LHVFLDPNVR NLVSEVSIKK LYAPKTPSNL
RICVVDCGMK YNQLRCFLKR GATVEVVPWD HPLDPSEYDG LFLSNGPGNP LMCATTIENV
KKAIESKKPI FGICLGHQLL AIASGCATYK MKFGNRGHNQ PCIHFSTKRC FMTSQNHGFA
VDSKSIPEGW IELFVNANDN SNEGLIHKNF PFFSVQFHPE HCAGPQDLEI LFDVFLSVVE
LHKNNSAYIS LVDKISEALQ FKQPLHTPLS HKRNKVLLLG SGGLSIGQAG EFDYSGSQAI
KALQEENIRT VLINPNIATV QTSKGLADKV YFLPLLPSYV EQVICSERPD GVLLNFGGQT
GLNCGVELQK NGVFDKYNVK VLGTPIQSII ETEDRKLFAD RISEIGGKVA PSAAVYCVNE
ALEAANRLGY PVLARSAFSL GGLGSGFANN DDELRKLAQH AFAHSNQLII DKSLKGWKEV
EYEVVRDAFD NCITVCNMEN VDPLGIHTGE SIVVAPSQTL TNAEYNRLRT TAIRVIRHFG
IVGELMYGRE LLGFSLKFHF TVNARLSRSS ALASKATGFP LAYVAAKLAL GYSLVDIRNS
VTATTTSCFE PSLDYCVVKI PRWDLSKFSR VSTKIGSSMK SVGEVMAIGR KFEEAFQKAM
RMVDENVIGF DPHAKSPCDV ELEQPTDKRM FVLAAAIKDG YTVDRLYELT KIDRWFLYKM
VNIVKMQMHL EEQTHVTVEQ LLEAKKLGFS DKQIASFVKS TELAIRKKRE ESGILPFVKQ
IDTVAAEWPA STNYLYLSYN GTSHDLNFPG GYTMVIGSGV YRIGSSVEFD WCAVGCLREL
KKLGKKTIMV NYNPETVSTD YDMCDRLYFE EISFEVVMDI YNVENPEGII LSMGGQLPNN
IAMDLHRQQA RILGTSPESV DGAENRFKFS RMLDRIGILQ PRY
//