CARB_LACPL
ID CARB_LACPL Reviewed; 1058 AA.
AC P77886; F9URI2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=pyrAB; OrderedLocusNames=lp_2700;
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=8982065; DOI=10.1016/s0378-1119(96)00461-1;
RA Elagoez A., Abdi A., Hubert J.-C., Kammerer B.;
RT "Structure and organisation of the pyrimidine biosynthesis pathway genes in
RT Lactobacillus plantarum: a PCR strategy for sequencing without cloning.";
RL Gene 182:37-43(1996).
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;
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 -!- ACTIVITY REGULATION: Inhibited by pyrimidines.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
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 -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; Z54240; CAA91005.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC79821.1; -; Genomic_DNA.
DR RefSeq; WP_011101886.1; NC_004567.2.
DR RefSeq; YP_004890335.1; NC_004567.2.
DR AlphaFoldDB; P77886; -.
DR SMR; P77886; -.
DR STRING; 220668.lp_2700; -.
DR EnsemblBacteria; CCC79821; CCC79821; lp_2700.
DR KEGG; lpl:lp_2700; -.
DR PATRIC; fig|220668.9.peg.2260; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_2_9; -.
DR OMA; IEPAGIH; -.
DR PhylomeDB; P77886; -.
DR BioCyc; LPLA220668:G1GW0-2312-MON; -.
DR UniPathway; UPA00070; UER00115.
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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 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 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; SSF48108; 1.
DR SUPFAM; SSF52335; SSF52335; 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; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1058
FT /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT large chain"
FT /id="PRO_0000145014"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT DOMAIN 671..861
FT /note="ATP-grasp 2"
FT DOMAIN 930..1058
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..546
FT /note="Oligomerization domain"
FT REGION 547..929
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 930..1058
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 697..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="K -> E (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..411
FT /note="PA -> ST (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="P -> Q (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="D -> G (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="R -> H (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="I -> V (in Ref. 1; CAA91005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1058 AA; 115757 MW; 3A5DEDF82EB60C55 CRC64;
MPKRTDIHKI MVIGSGPIII GQAAEFDYSG TQACLALKEL DYEVVLVNSN PATIMTDKEI
ADQVYLEPIT LEFVSQILRK EHPDAILPTL GGQQGLNMAM ELSKSGILDE LHIELLGTKL
SAIDQAEDRE QFKALMEELG EPVPASGIAR TVDEALAFAK QAGYPVIVRP AFTMGGTGGG
IAETPQQLHD ITENGLALSP VTQVLIEQSI AGYKEIEFEV MRDAADNAMV VCNMENFDPV
GIHTGDSIVY APVQTLADRE VQLLRDAALK IIRALKIEGG CNVQLALDPN SFNYYIIEVN
PRVSRSSALA SKATGYPIAK MAAKIAVGLH LDEIKNPVTG TTYAEFEPAL DYVVCKIPRW
PFDKFTHADR RLGTQMKATG EVMAIGRNIE EATLKAVRSL EIGVHHVEEP ALRSVDDDVL
SDKLIHAQDD RLFYLTEAIR RGYPIDELAE LTKINVFFLD KLLHIIEIEQ ALRTHTDDIE
TLTVAKRNGF ADQTVADYWH ETIDQVRDFR LAHKLAPVYK MVDTCAGEFA SETPYYYGTY
EFENESIVTK RPSVLVLGSG PIRIGQGVEF DYATVHSVKA IQKAGYEAII MNSNPETVST
DFSVSDKLYF EPLTIEDVLN VIELEKPVGV IVQFGGQTAI NLAKPLADHG IKILGTSVAD
VNRAEDRDEF DKVIKALAIP QPAGDTASDE ATALAIADKL GYPVLVRPSY VLGGRAMEIV
KKRTDLDYYM HNAVKVSHDH PVLVDSYLVG KECEVDAICD GQTVLIPGIM EHIERAGVHS
GDSMAVYPPQ SLSAAVQAQI VDYTEKLAIA LNCVGMMNIQ FVIHDDQVYV IEVNPRASRT
VPFLSKVTNI PMAQVATRAI LDQSLAEQGY QTGLVTPGPL VHVKAPVFSF SKLNRVDSLL
GPEMKSTGEV MGSDVTMAKA LYKAFEAAKL HVPSHGNVLL TVRDEDKPET VALAKRFHAL
GYQLLATRGT ATALTTHGLP VTTVDKIDSG ERDLLHRMEA GEIQVVINTV SDEEQAENDG
TLIRNTSIMH GIPLFTALDT VAAILQVRES QSFVTQAL
