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Database: UniProt
Entry: T1HLK0_RHOPR
LinkDB: T1HLK0_RHOPR
Original site: T1HLK0_RHOPR 
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
//
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