ID Q4N0R5_THEPA Unreviewed; 1680 AA.
AC Q4N0R5;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Glutamine-dependent carbamoyl phosphate synthase, putative {ECO:0000313|EMBL:EAN30784.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EAN30784.1};
GN OrderedLocusNames=TP03_0048 {ECO:0000313|EMBL:EAN30784.1};
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN30784.1, ECO:0000313|Proteomes:UP000001949};
RN [1] {ECO:0000313|EMBL:EAN30784.1, ECO:0000313|Proteomes:UP000001949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga {ECO:0000313|EMBL:EAN30784.1,
RC ECO:0000313|Proteomes:UP000001949};
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00043737};
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:EAN30784.1}.
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DR EMBL; AAGK01000005; EAN30784.1; -; Genomic_DNA.
DR RefSeq; XP_763067.1; XM_757974.1.
DR STRING; 5875.Q4N0R5; -.
DR EnsemblProtists; EAN30784; EAN30784; TP03_0048.
DR GeneID; 3499895; -.
DR KEGG; tpv:TP03_0048; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_03g00048; -.
DR eggNOG; KOG0370; Eukaryota.
DR InParanoid; Q4N0R5; -.
DR OMA; YEVEYLY; -.
DR Proteomes; UP000001949; 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:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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 Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
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; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAN30784.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 624..831
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1237..1428
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1494..1680
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1680 AA; 189651 MW; 7202EBA512578109 CRC64;
MSDQLQHLPW SPEELYVGPP AKLLLSDGRE FYGYSFGYED QESFNPQHLD TTGELVFSTS
MLGYAECVTD PNYSGQILVL TYPEIGNIGV PSDDTDEYGL LRNFESGSKY LRGLIVCNYT
IDPSHWLCVS TFSDFLKRKK VPAISGVDTR ALTKHLRTNG PLLGRIIIGN SKLYGPSYFN
SDHTQLLNKS CFYDRNTKSL AQLLHSEQLD QVSGNLYLYS FHTTNNYNKL VLKYTFQSSE
FGSLLNQLKR SDFHTVYHKN LTFNSMNLTQ DLVSKFLTSD TNSVMLLVVV DLGMKNSILR
SLLNNCPNNV RVLVVPHTVD FSVLDYDGLF LSNGPGNPNN YSDLVKTVGK CLTKQKPIFG
ICLGNLLLGL AAGYNCVKMH RGNYGANQPC IDLRTYKCYA TTQSHIYQLV TQNSKPTRWT
TLFENANDNT LEGLVNLDYP FFGVQFHPFS RPVYFDPDDP TKYHDLDTSF LYKDFFTCLL
KKTLIPIHIR MMSTHIRCKR ILLLSSGGLS IGQAGEFDYS GSQAIKALKE SDAKIILVNP
NIATVQTSKG MAHVTYFLPI TFEYVKQIIE KEKPDGIMCA FGGQTGLNVG IELYQKNVLI
DNNCEILGTS IKTIIDTEDR YLFNKKMTEI GERCAPSKEC TSIEECVTVA KDLGYPVLIR
GNFELGGFGS GFANNESELL EIVTRLFHSN RGKTSLKVLL NIFTDTCVHI DKSLKGWKEI
EFEVLRDNND NCVCAASMEN FDPLGVHTGD SIVVAPAQTL SASECSHLRQ VAFNVVRHLD
LVGECNIQFA VNPFKFEYFI VELNARLSRS SALASKATGY PLAYMAAKIA LGYDLVQMRN
SITLCTTACF EPSLDYVVVK MPRWDLRKFE NANNTIGSSM KSVGEVMGIG KTFEETMQKS
LRMVSDSILG FCSYSVEDLT REQVIKILEN PTPERVFAIY RAFELGITVQ QINEFTRIDN
WFLNRLHNIY LCSERLKKLT RKEELTHSQL LYYKVLGFSD RQMSLLINNK GNVVNLVNKS
ELEKYENEFR DYRLKLLVTP KVNIIDTLAA EYPVVTNYCY MTYNSTEHDI RPLNDKLYSK
IAETVDKDSS RSPSMRYRDD KFSPLNKEKY DRKTLDKDSI IVLGCGPYRI GSSIEFDWSA
VGCIKTLRRL GFFSIIVNCN PETVSTDFDV SDRLYFEELS LEIVDEIYRF ECPQGIILSV
GGQTANNLAI KLGELGLNIL GTPVSSIDKC ECRNKFSDIC DMLGIDQPSW EEFTCVDAAK
KFSNKVGFPV LARPSYVLSG ASMKVISSHK ELESFLQTSA IVNRSHPVVI TKFIENAKEV
EMDCVSKDGV IVNYAISEHV ENAGTHSGDA TLIIPAQNIH VDTHRRVKKI TQKLSKYLNI
TGPFNVQFMC KNNKIKVIEC NLRASRTFPL ITNTLNINFI ELATRVMVNA PFRVENVQLM
DLDYVAVKMP LFSFDRLYPA DPLLGVEMKS TGEIASFGYN KYEALLKAMT ASGMKIPERG
VLLSLGSTVN KFIFSRKIKG LLSLGLDVYA TEGTYDYIRK LWDSEQLFYN SDNEIDTQFM
SKLNLDDFEF DFEPTSMGEF KKVFKPTVQG TSNGTPDVYE LISNRKVDLL INVTDSINTL
YTSGGYMMRR AFVDAKISLI TSTKLATLVI DAMLYRKSKI SKGKDFIHIK SHQEYLSENC
//
