ID A0A2K3P243_TRIPR Unreviewed; 1160 AA.
AC A0A2K3P243;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carbamoyl-phosphate synthase large chain-like protein {ECO:0000313|EMBL:PNY09313.1};
GN ORFNames=L195_g005859 {ECO:0000313|EMBL:PNY09313.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY09313.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNY09313.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY09313.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNY09313.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY09313.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:PNY09313.1}.
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DR EMBL; ASHM01003063; PNY09313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3P243; -.
DR STRING; 57577.A0A2K3P243; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000236291; 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:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01424; MGS_CPS_II; 1.
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 HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 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; IPR033937; MGS_CPS_CarB.
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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000236291};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 202..397
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 759..952
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1019..1160
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1160 AA; 127075 MW; 13611B26F21273D6 CRC64;
MSIAYSITHF NKLPLHSSSS IFSPIPRFSS KPNLPFQISQ KPISFSAVVT PTATTTASTP
TPSPQTLTKV GKRTDIKKIL ILGAGPIVIG QACEFDYSGT QACKALREEG YQVILINSNP
ATIMTDPDMA DRTYVTPMTP ELVEQVLEKE RPDALLPTMG GQTALNLAVA LAESGVLEKY
GVELIGAKLE AIKKAEDREL FKQAMKNIGI KTPPSGTCST LDECMQIANE IEFPLIVRPA
FTLGGTGGGI AYNREDLMEI CKAGIAASLT NQVLIEKSLL GWKEYELEVM RDLADNVVII
CSIENIDPMG VHTGDSITVA PAQTLTDKEY QRLRDYSIAI IREIGVECGG SNVQFAVNPV
DGEVMVIEMN PRVSRSSALA SKATGFPIAK MAAKLSVGYS LDQIPNDITK KTPASFEPSI
DYVVTKIPRF AFEKFPGSQP ILTTQMKSVG ESMAVGRTFQ ESFQKAVRSL EYGHAGWGCG
PVKELDYDWE QLKYNLRVPN PERIHALYAA MKKGMQIDEI FELSFIDKWF LRQFKDLVDV
ENFLMSHKLS DLTDVDFYEV KRRGFSDKQI AFATKSNEKE VRDRRLSLGV VPAYKRVDTC
AAEFEANTPY MYSSYDFECE SAPTNRKKVL ILGGGPNRIG QGIEFDYCCC HASFSLQAAG
YETIMVNSNP ETVSTDYDTS DRLYFEPLTV EDVVNIIDLE RPDGIIVQFG GQTPLKLSLP
LQQYLDEHKP ECASGNGHVR IWGTSPDSID VAEDRERFNV MLHELQIEHP KGGIARSEAD
ALAIAADVGY PVVVRPSYVL GGRAMEIVYS DERLVTYLET AVEVDPERPV LIDKYLSDAV
EIDIDALADS HGNVVIGGIM EHIEQAGIHS GDSACSIPTR TVSAASLETI RSWTEKLAKK
LNVCGLMNCQ YAITPSGKVY LLEANPRASR TVPFVSKAIG HPLAKYASLV MSGKSLHDIN
FTKEVIPKHV SVKEAVLPFS KFPGCDVFLS PEMRSTGEVM GIDPLYNIAF AKAQIAAGQK
LPLSGSVFLS LNDLTKPHLE KIAKAFIDNG FQIVATAGTA LALKFCNIPA VLVLKLHEGR
PHAGDMIANG DIQLMVVTSS DDALDRIDGL ALRRMALDYK VPIVTTVNGA MATAEAIKSL
KSNSIKMIAL QDFIVDELKE
//
