CARB_LACLM
ID CARB_LACLM Reviewed; 1064 AA.
AC O32771; A2RK73;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
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=llmg_1089;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9721272; DOI=10.1128/jb.180.17.4380-4386.1998;
RA Martinussen J., Hammer K.;
RT "The carB gene encoding the large subunit of carbamoylphosphate synthetase
RT from Lactococcus lactis is transcribed monocistronically.";
RL J. Bacteriol. 180:4380-4386(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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 -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {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 pyrimidines.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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DR EMBL; AJ000109; CAA03928.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97683.1; -; Genomic_DNA.
DR RefSeq; WP_011834997.1; NZ_WJVF01000012.1.
DR AlphaFoldDB; O32771; -.
DR SMR; O32771; -.
DR STRING; 416870.llmg_1089; -.
DR EnsemblBacteria; CAL97683; CAL97683; llmg_1089.
DR KEGG; llm:llmg_1089; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_9; -.
DR OMA; IEPAGIH; -.
DR PhylomeDB; O32771; -.
DR BioCyc; LLAC416870:LLMG_RS05530-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000364; 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_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 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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1064
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145013"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 671..861
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 930..1064
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..1064
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 697..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT CONFLICT 32
FT /note="Q -> E (in Ref. 1; CAA03928)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="R -> G (in Ref. 1; CAA03928)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="G -> V (in Ref. 1; CAA03928)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="P -> H (in Ref. 1; CAA03928)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="E -> L (in Ref. 1; CAA03928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 117429 MW; EEBB4A4CA0DBDAB5 CRC64;
MPKRNDIKKI MIIGSGPIII GQAAEFDYAG TQACLALKEE GYEVVLVNSN PATIMTDREI
ADTVYIEPIT LEFVSKILRK ERPDALLPTL GGQTGLNMAM ELSKTGILEE LNVELLGTKL
SAIDQAEDRE LFKELCESIN EPLCASDIAT TVEEAINIAD KIGYPIIVRP AFTMGGTGGG
ICDTEEELRE IVANGLKLSP VTQCLIEESI AGYKEIEYEV MRDSADNAIV VCNMENFDPV
GVHTGDSIVF APSQTLSDNE YQMLRDASLN IIRALKIEGG CNVQLALDPN SYEYRVIEVN
PRVSRSSALA SKATGYPIAK MSAKIAIGMT LDEIINPVTN KTYAMFEPAL DYVVAKIARF
PFDKFENGDR HLGTQMKATG EVMAIGRNIE ESLLKAVRSL EIGVFHNEMT EAIEADDEKL
YEKMVKTQDD RLFYVSEAIR RGIPIEEIAD LTKIDIFFLD KLLYIVEIEN QLKVNIFEPE
LLKTAKKNGF SDREIAKLWN VTPEEVRRRR QENKIIPVYK MVDTCAAEFE SSTPYFYSTY
EWENESKRSD KEKIIVLGSG PIRIGQGVEF DYATVHCVKA IQALGKEAIV INSNPETVST
DFSISDKLYF EPLTFEDVMN VIDLEEPLGV IVQFGGQTAI NLAEPLSKAG VKILGTQVED
LDRAEDRDLF EKALQDLDIP QPPGATATNE EEAVANANKI GYPVLIRPSF VLGGRAMEII
NNEKDLRDYM NRAVKASPEH PVLVDSYLQG QECEVDAICD GKEVLLPGIM EHIERAGVHS
GDSMAVYPPQ NLSQAIIDTI VDYTKRLAIG LNCIGMMNIQ FVIYEEQVYV IEVNPRASRT
VPFLSKVTNI PMAQLATQMI LGENLKDLGY EAGLAPTPDM VHVKAPVFSF TKLAKVDSLL
GPEMKSTGEA MGSDVTLEKA LYKSFEAAKL HMADYGSVLF TVADEDKEET LALAKDFAEI
GYSLVATAGT AAFLKENGLY VREVEKLAGG EDEEGTLVED IRQGRVQAVV NTMGNTRASL
TTATDGFRIR QEAISRGIPL FTSLDTVAAI LKVMQSRSFT TKNI
