ID K0DC69_LEUCJ Unreviewed; 837 AA.
AC K0DC69;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:AFT81536.1};
GN OrderedLocusNames=C270_03115 {ECO:0000313|EMBL:AFT81536.1};
OS Leuconostoc carnosum (strain JB16).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT81536.1, ECO:0000313|Proteomes:UP000006299};
RN [1] {ECO:0000313|EMBL:AFT81536.1, ECO:0000313|Proteomes:UP000006299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB16 {ECO:0000313|EMBL:AFT81536.1,
RC ECO:0000313|Proteomes:UP000006299};
RX PubMed=23144413; DOI=10.1128/JB.01805-12;
RA Jung J.Y., Lee S.H., Jeon C.O.;
RT "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT from Kimchi.";
RL J. Bacteriol. 194:6672-6673(2012).
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 -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003851; AFT81536.1; -; Genomic_DNA.
DR RefSeq; WP_014974149.1; NC_018673.1.
DR AlphaFoldDB; K0DC69; -.
DR STRING; 1229758.C270_03115; -.
DR KEGG; lcn:C270_03115; -.
DR PATRIC; fig|1229758.3.peg.623; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_1_9; -.
DR Proteomes; UP000006299; Chromosome.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
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; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
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:UP000006299}.
FT DOMAIN 136..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 837 AA; 93941 MW; 137E18E476CCD099 CRC64;
MSNTITNNKI KKVLFIGAGA NDFGREGEHD AAIFQVMPEL RGHGIEIFII DDNPYALSLE
SLAATVFWQQ LTVDNLKKVV RENNIDTVAP LFGGESSLRL WAEVVQSWAH GDGTVPSTLG
LSIDMLLKVN NIPALTAMMA DIGLPVINNY VLKAQDEANE LLRELHLPLM VRALHPNQTN
TRQIVERLDD FEDAINLAKT QSVTQEVIIS RAINGLKEVS IEILRDVRGN KMQIGASEDM
DPIGIHTADS LSVSPILTIQ DQLIGRMRDY AFRIADMLQL KGVMHVQFAV DDDTHTIYVI
KVSPYIDQMA TRMSLATGYP TMLVAINLAI GVPLEEIVLP HDFGKHVAMM EPMMDHVVVK
LPVFPFGELE AAGVHVNRQL NSVQKSVGST LGLGRTFIEA LEKAIRSAHF NNASFSPTNM
KHINDDELIQ QLIHPQDNRV LLLIEAIKRG YEIDELAELT AIDEFYFYQL KYLHQLESEI
ETNIDNIDAL RLGKKYGLSD GLIARFWHTD FNIIRTLAKE NGINVTYKSV EPSAGEFPEN
ARQYYATYES ENESVQISDN TVLVIGSGAF RMGDAAAGGY ATTVVMSELR RLQYPTIIMN
NNPSDATLLP HLADKQYLEP LEVSDVMKVV ELEKPKVIVI PGNRRKLINA LRDLNQNVVI
LPKTKHIPGG PNENQSEFAL NIFYDGQQAY PINLTQHMAG EMRVIPQVAH IPDTILSTNF
EAPGVYQVIY YQSIVHWVDR MDLSNMGYDS WIRPMPFGQV AYLSKAMQTQ WLRLTIRAAM
DDLTSRDIEL LQTINERPIV YPYSMIAADI NYRLHLQPHE VIDGTRFEMG VGVKDYG
//