ID H3GA51_PHYRM Unreviewed; 1588 AA.
AC H3GA51;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0008006|Google:ProtNLM};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra71989, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra71989}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra71989};
RG EnsemblProtists;
RL Submitted (JUN-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; DS566064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3GA51; -.
DR EnsemblProtists; Phyra71989; Phyra71989; Phyra71989.
DR VEuPathDB; FungiDB:PSURA_71989; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_0_1_1; -.
DR InParanoid; H3GA51; -.
DR OMA; WSPFNGK; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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 HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
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; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 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 SMART; SM00851; MGS; 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; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 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:UP000005238};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 530..728
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1077..1267
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1333..1479
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 279
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1588 AA; 174032 MW; 50A5F428098292F3 CRC64;
MSSVSFSEPA TQTLSPVANI INEDDASRGT LVLADGTTYA GYSFGADKSM SGEVVFNTGM
VGYPEALSDP SYRGQILVLT YPLIGNYGVP DMDVQDAFGL PKFFESSTVQ ISGLIVSEYS
FQHSHWNAVK SLGDWLKEHN VPALFGIDTR MITKRIRSLG AVLGKIEFDG QPADIVDPNK
LNLVAQVTTK EVTVYNKGAS PKIVAFDCGM KHNIIRYLVS KGVELTVVPY DYDLPSSELQ
YDGIFISNGP GDPIMASKTI DSIRWAINLE NPKPIFGICL GNQILALAAG ATTYKMKYGN
RGMNQPCIDM RTTRCYITPQ NHGYAVDSSS LPAGWKTFFM NANDKSNEGI IHEHKPFFSV
QFHPEACGGP TDTAFLFDMF LEKVNNAPPK LTVMDTSLYD RPTFSKVLLL GSGGLSIGQA
GEFDYSGSQA IKALREEGVH VILVNPNIAT VQTSKGLADK VYFVPVRAET VLEIIKKEKP
DGILVSMGGQ TALGVGIELY LNGDLERHNV RVMGTQIESI IDTEDREKFS AKLDEIGETI
ALSHPATTVE GALKAAHDIG YPVLVRSAFA LGGLGSGFAA NDEELTVLAT KALHGSASKG
SIKQILIDQD LRGWKEVEYE VVRDAKDNCI TVCNMENFDP LGIHTGDSIV VAPSQTLSNS
EYFKLRSTAQ KVVRHLNIVG ECNIQYALDP HSERYCIIEV NARLSRSSAL ASKATGYPLA
YVATKISLGI DLVTIKNSVT KTTTACFEPS LDYCVVKMPR WDLKKFSRVS NDLGSYMLSV
GEVMSIGRNF EECIQKAVRM VNPNLDGLEG SPVDNETNPE VLDAQLSHPT DERLFYVIAA
LDAGYTIDRV HQLTKIDKWF LSKLARISSL RQSVPKFTLD TLSERFIRTL KVNGFSDRQI
AAKLPNATAM QVRELRKQMG VVPCVKQIDT LAAEFPAQTN YLYMTYGGSE DDIPASEESI
VVLGCGAYCI GSSVEFDWCG VSAVRTVREL GKPAIVVNYN PETVSTDYDE SDRLYFEELS
LERVLDIYDR EQPEGVIVSV GGQIPNNLAM PLSKAGVNIL GTSPESIDQC EDRNKFSALL
DTLGVDQPRW AEVKEVDAAL EFAKEVQYPV LVRPSYVLSG AGMIVALDEE QLRAYLNTDA
VKISRSISVS KFILNAKEIE FDGVAKDGAI LNYAMSEHVE NAGVHSGDAT LVLPAQKLYV
GTIKQVKRIA SAIASALNIT GPFNIQLMAK ANDVKVIECN LRASRTFPFI SKTFDLNFIN
LATKAMIGLP VKSVPIALID IDYVGVKAPQ FSFTRLHGAD PSLGVEMAST GEVACFGTDM
HEAYLKALLS AGFKMPKEKK VLISIGNQDI RREFAEGALI LQELGYTIYA TPGTSEYLAT
QGVQTIALRK PSDPESDLPS VIEYISSGKI ELVINVPEGA NREELTSGYK IRRAAVDFGV
SLINNVKCAL LFAQAVQKRS RRLNAVRQRK RRHRRFVYAV AEGLHRSKRA QLGAVALQLM
HTLLTLLSQR LLHLFRCVLK LLRVALLDRL ALTGKGALQL RQKRRTLLAH VARQIISVLL
LESSHLVARL AGKDLLLQTQ LTGKQLLV
//
