ID A0A0L6VIS0_9BASI Unreviewed; 1182 AA.
AC A0A0L6VIS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carbamoyl-phosphate synthase arginine-specific large chain {ECO:0000313|EMBL:KNZ60681.1};
GN ORFNames=VP01_1519g2 {ECO:0000313|EMBL:KNZ60681.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ60681.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ60681.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ60681.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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:KNZ60681.1}.
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DR EMBL; LAVV01005775; KNZ60681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6VIS0; -.
DR STRING; 27349.A0A0L6VIS0; -.
DR VEuPathDB; FungiDB:VP01_1519g2; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 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:UP000037035};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 241..436
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 750..948
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1016..1179
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1182 AA; 130874 MW; 5E11161422879706 CRC64;
MIRASLPLKR FYSARQLPHS TFQSVPAQVS FRGFSHPKQM ALSISASRHQ DPKVVQPTLS
TPSEIAKKIS AAVLPKIDKP DVKKVLVVGS GGLSIGQAGE FDYSGSQAIK ALRESNIETI
LINPNIATIQ TSHHLASEVY FLPVTADYVA WVLEKERPDG ILLTFGGQSA LNVGIQLDKM
GILERLGVQV LGTPISTLIV SEDRDLFVKA LNGMSMALIP KNFFDTMFLQ LTSCELAHFS
SAISVEIDIP AAHSTAVSTI SDALNAAKEI GYPVILRSAF SLGGLGSGFA QNEEELRDLS
AKSLSLSPQV LIEKSLKGWK EVEYEVVRDA ADNVIICCNM ENFDPLGTHT GDSIVVAPSQ
TLSDDDYHML RSAAIKIYAL NPHKREYMVI EMNARLSRSR QVIALGHTLP ELPNAVTKTT
TACFEPSLDY VVTKIPKWDL KKFQYVNREV GSAMKSVGEV MAIGRTFEES IQKAIRQIDP
NYHGFEAYIK PKDLDHALSI PTDTRLFAVA YAMLVENYSV AKIYELTKIT KWFLYKLDNI
VQCHRKLKSL QSIDLVDEEL MRSSKKLGFS DRQIADLVSS TEDKVRAKRH SLGVKPFVKR
IDTLAAEYPA HTNYLYTTYH ATEHDLEFDE HGTMVLGSGV YRIGSSVEFD WCAVTCVRKV
REMGKRTVMI NYNPETVSTD FDEADRLYFE ELGYERVMDI YELESAQGVI VSVGGQLPQN
IALRLKQNGV KVLGTDPEMI DNAEDRHKFS STLDAVGVDQ PDWVEVTSLE SAVKFADEVG
YPVLIRPSYV LSGAAMNVVW DRTTLEYSLT AAAEVSSEHP VVVTKFIDGA QEIDVDAVAH
KGELIVHAVS EHVENAGVHS GDATLVLPPF TLSDKEMARL KQISQKVAKA LKISGPFNMQ
IIRQESEEPN GESRLKVIEC NLRASRSFPF VSKVLGANFI DIATAAILGE NVPKPMDLMA
EKRDYCAIKV PQFSWTRLAG ADPFLGVEMA STGEVASFGR DVHEAYWASL LSTNGFKLPK
ANSGILIGGD TTQPELKYCA ETLSKLGFKL YCSSPEVEAF FESLKAKDPI GTSIIPVKRI
EFPKRDKRKL REVFEEYEIQ CVINLAKQRG RDVLDEDYVA RRNSVDFGLP LINNNKCARL
FVEALAKKIP LGGLKPYAEG KIPSEVRSWS EFVGLAKGNR PV
//
