ID W2PVS0_PHYPN Unreviewed; 1511 AA.
AC W2PVS0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=carbamoyl-phosphate synthase (ammonia) {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
GN ORFNames=PPTG_14525 {ECO:0000313|EMBL:ETN04736.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN04736.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN04736.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN04736.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI669603; ETN04736.1; -; Genomic_DNA.
DR RefSeq; XP_008910130.1; XM_008911882.1.
DR STRING; 761204.W2PVS0; -.
DR EnsemblProtists; ETN04736; ETN04736; PPTG_14525.
DR GeneID; 20183808; -.
DR VEuPathDB; FungiDB:PPTG_14525; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000018817; 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 CDD; cd01423; MGS_CPS_I_III; 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:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 553..745
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1094..1285
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1356..1501
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 379
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1511 AA; 166318 MW; C1E60886A6F9457E CRC64;
MLRLSHSVKR RVPLHKASGN RLLVSAREKV DRRNAPRFET PAVLEFEDGT RFHGVSFGAK
KSMAGEVVFT TGMVGYPEAL TDPSFKGQIL NMTFPMIGNY GVPDTKALDE FGLNKNIESD
RIHAAGMIVQ DYSNHHSHWN AAQSLSEWLE SEGIPGIAGI DTRAITKKIR AHGAMAGRII
VEGSDKPNLV DVNEANLASL VSTKEVITYG KGNPLKILAV DCGIKYNIIR ELVKRGAEVK
RVPWNHDISS EIGWYDGLFI SNGPGDPAIM KETTAQLKKA LALQGDDVKP IFGICLGNQL
LSQAAGATTY KLPFGNRGQN QPVHNLKTGQ SYITAQNHGY AVDGKTLPSD WEELFVNLND
GTNEGIIHKS KPYFTAQFHP EHAGGPTDTE FLFDTFLDAV RNKEKGPIKS LVQRPHIERP
TVKKVLVLGS GGLSIGQAGE FDYSGSQAIK ALKEENIETI LINPNIASVQ TNIDRSSEAQ
ASNVYYLPVN PEFVEQVIKR ERPDGILISM GGQTALNCGV ELDKRGVFKK YGVQVLGTQI
DVINYTEDRE LFNDKLAEIN EKIAQSEAVE SVEDAVKAAY HIGFPVMIRS AFALGGLGSG
ICEDEAQLRK MAKQAFSGSP QILVERSMKG WKEVEYEVVR DAANNCLTVC NMENFDPLGI
HTGESIVIAP SQTLSNREYH MLRETAVKVV RHLGIVGECN IQYALNPESE EYCIIEVNAR
LSRSSALASK ATGYPLAFVA AKLALGINLP DLKNSVTKST TACFEPSLDY CVAKMPRWDL
AKFDNVSTEI GSSMKSVGEV MSIARTFEEA IQKALRMVEP SNEGFEPRYD ELSHDELVKA
LGKPTDRRIY QIAQALKTGQ LSIEQVHEIT KIDTWFLSRL QAICDCDVNL TGKKLNEVTG
EEIVEAKKLG FSDRQLARMF SCTDDGVRAK RKELGIVPAV KQIDTLAAEY PAQTNYLYMT
YNGTEHDVAA QDPNDGVMVL GSGAYRIGSS VEFDWCAVSC IRTLRKLGHR AVMLNYNPET
VSTDYDECDQ LYFEELSKER VMDVNDREGV QGVVVSVGGQ IPNNLALPLH KAGVKVLGTH
PTMIDSAEDR YKFSKLMDEA GVPQPAWKEL TSHAAAREFA ERVGYPVLVR PSYVLSGAAM
NVAYSFDELD NVLNQAVAVS ADHPVVITKF VEGAKELELD AVAKDGKVIA AAISEHVENA
GVHSGDATLV LPPVQASSFY TNQIKRNAEK IAKALNISGP FNAQFLAKGA DVSVIECNLR
ASRSFPFVSK TTGADFINAA TKVMVGHSTE NDNLPPLDGP KRPEGYVGIK SPMFSYTRLG
GADPLLGVEM ASTGEVACFG KNRHEAFLKA LISSNFKLPE KNILLSMQDK FSEEFVHAAY
KMHELGYNLY TTEKTHAYLK KYDIPSTKVD FPSDGDSENN ALNLIKDGKI DLVVNLPNNQ
SQQTENNYLI RRTAVDFSIP LLTNISLVQL FVEAMAIHKN KPMLGLEPDS LFDYYKREKE
EDAWTDVHEF H
//
