ID V9FLN5_PHYPR Unreviewed; 1032 AA.
AC V9FLN5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:ETI52380.1};
DE Flags: Fragment;
GN ORFNames=F443_04453 {ECO:0000313|EMBL:ETI52380.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI52380.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI52380.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI52380.1,
RC ECO:0000313|Proteomes:UP000018721};
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 P1569.";
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};
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:ETI52380.1}.
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DR EMBL; ANIZ01000811; ETI52380.1; -; Genomic_DNA.
DR AlphaFoldDB; V9FLN5; -.
DR EnsemblProtists; ETI52380; ETI52380; F443_04453.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 2.
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; 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; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
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 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; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 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; PS51855; MGS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; 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:UP000018721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 70..268
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 617..807
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 873..1032
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETI52380.1"
SQ SEQUENCE 1032 AA; 113350 MW; 8D17F8CA25092C6A CRC64;
VYFVPVRAET VLEIIKKEKP DGILVSMGGQ TALSVGIELY LNGDLERHNV RVMGTQIESI
IDTEDREKFS AKLAEIGETI ALSQPATTVE GALKAANEIG YPVLVRSAFA LGGLGSGFAA
NDEELRVLAT KALHGSASKG QIKQILIDQD LRGWKEVEYE VVRDAKDNCI TVCNMENFDP
LGIHTGDSIV VAPSQTLSNS EYFKLRSTAQ KVVRHLGIVG ECNIQYALDP KSERYCIIEV
NARLSRSSAL ASKATGYPLA YVATKISLGI DLVSIKNSVT KTTTACFEPS LDYCVVKMPR
WDLKKFSRVS NDLGSYMLSV GEVMSIGRNF EECIQKAVRM VNPNLDGLDG SAVDNETNPE
VLDAQLSHPT DERLFYIISA LDAGYTVDRV HELTKIDKWF LSKLARISSL RQSVPKFTLD
TLSERFVRTL KVNGFSDRQI AAKLPNATAM QVRERRKQLG VLPCVKQIDT LAAEFPAQTN
YLYMTYGGSE DDIPTSEEAI VVLGCGAYCI GSSVEFDWCG VSAVRTVREL GKPAIVVNYN
PETVSTDYDE SDRLYFEELS LERVLDIWDR ENPEGVIVSV GGQIPNNLAM PLSKAGVNIL
GTSPESIDQC EDRNKFSALL DTLNVDQPRW TEVTDLNSAL EFAQEVQYPV LVRPSYVLSG
AGMIVASDED QLRDYLSSDA VKMSRSITVS KFILNAKEIE FDGVAKDGAI LNYAMSEHVE
NAGVHSGDAT LVLPAQKLYV GTIKQVKRIA SAIAQALDIT GPFNIQLMAR ANDVKVIECN
LRASRTFPFI SKTFDLNFIN LATKAMIGLP VKSVPIALID IDYVGVKAPQ FSFTRLHGAD
PSLGVEMAST GEVACFGTDM HEAYLKALLS AGFKMPKEKK VLISIGNQDI KREFAEGALI
LQELGYTIYA TPGTHEYLTT QGVKSIALRK PSDPESDLPS VIDYISSGKI ELVINVPEGT
NREELTSGYK IRRAAVDFGV SLINNIKCAL LFAQAMQKVR KLEICNIAEY YAMPTIGWRP
GQKLTARKMS IF
//
