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Database: UniProt
Entry: K0DC69_LEUCJ
LinkDB: K0DC69_LEUCJ
Original site: K0DC69_LEUCJ 
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}.
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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
//
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