ID F0W4K0_9STRA Unreviewed; 1543 AA.
AC F0W4K0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE SubName: Full=PREDICTED: similar to Carbamoylphosphate synthase p {ECO:0000313|EMBL:CCA16033.1};
GN Name=AlNc14C17G1820 {ECO:0000313|EMBL:CCA16033.1};
GN ORFNames=ALNC14_021760 {ECO:0000313|EMBL:CCA16033.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA16033.1};
RN [1] {ECO:0000313|EMBL:CCA16033.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA16033.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FR824062; CCA16033.1; -; Genomic_DNA.
DR EnsemblProtists; CCA16033; CCA16033; ALNC14_021760.
DR HOGENOM; CLU_000513_0_1_1; -.
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; 3.30.1490.20; 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:SF53; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 584..776
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1125..1316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1387..1532
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1543 AA; 170607 MW; F66D2AD106602E99 CRC64;
MSLETLRDTT QTNRSFTLFN QRIVVRYCHF KMLRVSQSLR KQVVQSRATG NRLCLSTSKK
VDRRNAPRFE TKAVLEFEDG SKYQGYSFGA PRSTSGEVVF TTGMVGYPEA LTDASFKGQI
LNMTFPMIGN YGVPCTKTLD SIGLNKYIES DRIHAAGMIV QDYSSVYSHW NASSSLSEWL
VRESIPGIAG IDTREITKKI RSKGAMAGRI IVGDETPPQF QDPNQQNLVA MVSTKEVRVF
GKGNPLKILA IDCGIKYNII RSLVSRGAEV KLVPWNHDVA SEAHWYDGLF ISNGPGDPAL
LEETTRHLRS ALNAEGDAVK PIFGICLGNQ LVGRAVGAET YKLPFGNRGH NQPVNNLKTG
LSYITSQNHG YALDGKSLPS EWEELFVNGN DGTNEGIIHK SKPMFTAQFH PEHCGGPTDT
EFLFDIFLDA VRRKEKGPIT SLVRAPVIER PQVQKVLVLG SGGLSIGQAG EFDYSGSQAI
KALKEENIET ILINPNIASV QTNIDKSSEA QASNVYYLPV TTDFVEQVIK RERPDGILIS
MGGQTALNCG VELHKRGILQ KYGVRVLGTQ IDVIDATEDR EKFNTKLKEI GEKIAESYAV
NSVEDAVVAA HKIKFPVMIR SAFALGGLGS GICETEKDLR SMATKAFSGS PQILVEKSMK
GWKEVEYEVV RDTANNCLTV CNMENFDPLG IHTGESIVIA PSQTLSNREY HMLRETAINV
VRHLGIIGEC NIQYALNPHS EEYCIIEVNA RLSRSSALAS KATGYPLAFV AAKLALGINL
PELKNSVTKS TTACFEPSLD YCVTKIPRWD LSKFDNVSTE IGSSMKSVGE VMSIARTFEE
GIQKALRMVE PSIKGFEPRN AEISREELVQ GLSRPTDKRI YQMAYALKHG VLSVDEIHDI
TKIDIWYLSR LQRIVDCDVN LTDRALADVS SMELKEAKQL GFSDRQLARM FRCSDDDVRA
RRKQCGVLPV VKQIDTLAAE YPAQTNYLYT TYNGTENDVA AQKPNDGVLV LGSGAYRIGS
SVEFDWCAVS CIRTLRKLGY RAVMLNYNPE TVSTDYDECN QLYFEELSKE RVMDVYEREG
VQGVVVSVGG QIPNNLALPL HKVGVKIMGT HPTMIDSAED RYKFSKLMDE AGVRQPAWKE
LTSMPAALKF ANSVGYPCLV RPSYVLSGAA MNVAYNDHDL ERVLGEAVDV SAEHPVVITK
FIEGAKELEL DAVARNGEII AAAISEHVEN AGVHSGDATL ILPPVEASSF YLNQIRQCGK
KIAMALNISG PFNAQFLAKG ADVSVIECNL RASRSFPFVS KTVSADFIQA ATKVMVGEPT
ESDNLPPLFG PKRPEGYVGI KAPMFSYTRL GGADPLLGVE MASTGEVACF GKNRPEAFLK
ALLSSNFKLP KENILLSMQD KFSDDFIHAA YQLHELGYNL FATDKTHTFL HKYDIPSTKV
DFPRDGDSEH DVINFIKEGK IDLVVNLPNS ESKQLKNNYL IRRTAVDFSI PVLTNISLVK
MFAEAMAIHK KKPLLGLDAD SLFDYYERED REKKAWTGVN EFH
//