ID M7Z423_TRIUA Unreviewed; 1152 AA.
AC M7Z423;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:EMS47095.1};
GN ORFNames=TRIUR3_35237 {ECO:0000313|EMBL:EMS47095.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS47095.1};
RN [1] {ECO:0000313|EMBL:EMS47095.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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}.
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DR EMBL; KD266071; EMS47095.1; -; Genomic_DNA.
DR AlphaFoldDB; M7Z423; -.
DR STRING; 4572.M7Z423; -.
DR eggNOG; KOG0370; Eukaryota.
DR OMA; FPFNKFP; -.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblPlants.
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 GO; GO:0016036; P:cellular response to phosphate starvation; IEA:EnsemblPlants.
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};
KW 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};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 1152 AA; 125794 MW; 965704108108DB46 CRC64;
MTKELGHTED DRDDSVTSIL DPNKICKNLL KIRFMDTAVT VRHFAAEPTK GGKLAGVKKI
MILGAGPIVI GQACEFDYSG TQACKALVEE GYEVVLVNSN PATIMTDPDL AHRTYIGPMT
PPLVEGIIAN ERPDALLPTM GGQTALNLAV SLAESGALDR LGVRLIGASL PAIRAAEDRQ
LFKQAMDRIG LKTPPSGIGT TLEECLAIAK DIGEFPLIVR PAFTLGGTGG GIAYNRAEFE
DICRSGLAAS HTQQVLVEKS LLGWKEYELE VMRDMADNVV IICSIENIDP MGVHTGDSIT
VAPAQTLTDK EYQRLRDHSV AIIREIGVEC GGSNVQFAVN PADGEVMVIE MNPRVSRSSA
LASKATGFPI AKMAAKLSVG YTLDQIPNDI TKKTPASFEP SIDYVVTKIP RFAFEKFPGS
EPILTTQMKS VGESMALGRT FQESFQKAVR SLETGFAGWG CAPIKELDWD WEKIKYSLRV
PNPDRIHAVY AAFKKGMRVE DIHEISFIDK WFLTELKELV DVEQFLISNN LDQLSKDDFY
QVKRRGFSDK QIAFATSSSE SDVRARRSAL GVTPTYKRVD TCAAEFEANT PYMYSSYEYE
CESAPTNRKK VLILGGGPNR IGQGIEFDYC CCHASFALRE AGYETIMMNS NPETVSTDYD
TSDRLYFEPL TVEDVTNVID LERPDGIIVQ YGGQTPLKLA LPIQRHLEEK KLRSASGTGF
VKIWGTSPDS IDAAEDRKRF NAILEELGIE QPKGGIARSE SDALSIASEV GYPVVVRPSY
VLGGRAMEIV YNDEKLIKYL ATAVQVDPER PVLVDKYLND AIEIDIDALA DSVGNVVIGG
IMEHIEQAGI HSGDSACSLP TRTVSTKCLD IIRSWTTKLA KRLNVCGLMN CQYAITPTGE
VYLLEANPRA SRTVPFVSKA IGHPLAKYAS LIMSGVTLPE LGFTKEVIPK HVSVKEAVLP
FEKFQGCDIL LGPEMRSTGE VMGIDYEFSG AFAKAQIAAG QILPVSGTVF VSLNDLTKRH
LAEIGRGFRE LGFNIIATSG TAKVLQLEGI TVEPVLKIHE GRPNARDMLK NGQIQVMVIT
SSGDDLDSRD GLQLRRLALA YKVPIITTVD GARATMDAIK SMKNKSIEIL ALQDYFQPAD
APQKLPAAQV AP
//
