CARY_LACPL
ID CARY_LACPL Reviewed; 1020 AA.
AC Q9RLS9; F9UL01;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; OrderedLocusNames=lp_0526;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX PubMed=9098069; DOI=10.1128/jb.179.8.2697-2706.1997;
RA Bringel F., Frey L., Boivin S., Hubert J.-C.;
RT "Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA
RT gene and the argCJBDF cluster are divergently transcribed.";
RL J. Bacteriol. 179:2697-2706(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX PubMed=10852872; DOI=10.1128/jb.182.12.3416-3422.2000;
RA Nicoloff H., Hubert J.-C., Bringel F.;
RT "In Lactobacillus plantarum, carbamoyl phosphate is synthesized by two
RT carbamoyl-phosphate synthetases (CPS): carbon dioxide differentiates the
RT arginine-repressed from the pyrimidine-regulated CPS.";
RL J. Bacteriol. 182:3416-3422(2000).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- INDUCTION: Repressed by arginine.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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DR EMBL; X99978; CAB56843.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC78016.1; -; Genomic_DNA.
DR RefSeq; WP_011101042.1; NC_004567.2.
DR RefSeq; YP_004888530.1; NC_004567.2.
DR AlphaFoldDB; Q9RLS9; -.
DR SMR; Q9RLS9; -.
DR STRING; 220668.lp_0526; -.
DR EnsemblBacteria; CCC78016; CCC78016; lp_0526.
DR KEGG; lpl:lp_0526; -.
DR PATRIC; fig|220668.9.peg.434; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_2_9; -.
DR OMA; HCFYRPN; -.
DR PhylomeDB; Q9RLS9; -.
DR BioCyc; LPLA220668:G1GW0-437-MON; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; IPR016185; PreATP-grasp_dom_sf.
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; SSF48108; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51855; MGS; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1020
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000145015"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 669..858
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 927..1020
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..544
FT /note="Oligomerization domain"
FT REGION 544..927
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 928..1020
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 695..752
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 818
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 831
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT CONFLICT 81
FT /note="A -> T (in Ref. 1; CAB56843)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Y -> C (in Ref. 1; CAB56843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 108911 MW; 5015DF9BFC8F6F08 CRC64;
MPKNNAIHSI AVIGSGPIKI GQAAEFDYAG TQACLSLKAA GYHVILINSN PATIMTDTAT
ADEVYLEPLT LTSVTKILRA AHPDALLPTL GGQTGLNLAM ALDQAGVLNE LKIQLLGTSL
ATINQAEDRA AFKTLMKRLH QPIPASTTVH HVTSALSFAE KIGYPVIVRP AFTLGGSGGG
IANNAAELTQ TLQRGLTMSP VTECLIEQSI AGFKEIEFEV MRDNQGTKII VCSMENFDPV
GIHTGDSIVY APVQTLTDTE YQQLRTAALT IVEALDIRGG YNVQLAQDPN SRQYYVIEVN
PRVSRSSALA SKATGYPIAK IAADIAIGLN LSEIKNPVTQ TTYAAFEPAL DYVVAKIPRF
AFDKFPTADA HLGTQMKATG EVMAIGSTLE EATLKAIASL EIDPKTQASL TPDHHVTTTE
YIDQLTHPTD QRLFYLLAAL QAGWPLAKLA TLTQITPFFL SKLQHIAQLI RNIKQVPTSQ
HLLSAKKYGV SLATMAHYAQ TSVATIAAMT ADLPFVYKMV DTCAGEFASV TPYFYSTAFG
QTNESHPLGH SILVLGSGPI RIGQGIEFDY TTVHCVKAIQ QAGYHAIIVN NNPETVSTDF
STSDKLYFEP LTIERLMPII ALEQPAGVIV QFGGQTAINL AHQLTKLGVT VLGTSVSATD
LTEDRQSFAD CLRLLKIAQA AGTTVTELSG ARQAAHAIGY PLLVRPSFVL GGRAMAIVHN
DHELTPVIKS AVAAGHGAPI LMDQYLAGTE CEVDVLSDGT SCFIPGIMEH IEGAGVHSGD
SITVYPPQHL SPAVQDKIVT IATKLAQHLH CVGMMNIQFV VTDDVYVIDV NPRASRTVPY
MSKVTHLPLA QLATRLILGQ SLATLGLVPG LLTPAPQQIA IKAPVFSFNK LPQSPVVLSP
EMKSTGETLG IGPTFTTAWH AAMADSYHLE TWQTVDGLIT DIATVAQPAV QELFAANHLT
VTTIANTTDW PAKTKAVGFT LNDQPDNPVA IAALNHGQPL ITAIDTLKTL LAVTPTPATI
