ID CARB_STRA3 Reviewed; 1060 AA.
AC Q8E5F5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 13-FEB-2019, entry version 106.
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};
GN OrderedLocusNames=gbs1077;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L.,
RA Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P.,
RA Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing
RT invasive neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000255|HAMAP-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
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
DR EMBL; AL766848; CAD46736.1; -; Genomic_DNA.
DR RefSeq; WP_001126464.1; NC_004368.1.
DR ProteinModelPortal; Q8E5F5; -.
DR SMR; Q8E5F5; -.
DR PRIDE; Q8E5F5; -.
DR EnsemblBacteria; CAD46736; CAD46736; CAD46736.
DR KEGG; san:gbs1077; -.
DR eggNOG; ENOG4105CU6; Bacteria.
DR eggNOG; COG0458; LUCA.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; AVFPFNK; -.
DR BioCyc; GCF_000196055:G1EE8-1185-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000823; 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; 3.40.50.1380; -; 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; 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 Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT CHAIN 1 1060 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145047.
FT DOMAIN 133 327 ATP-grasp 1. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 671 861 ATP-grasp 2. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 930 1060 MGS-like. {ECO:0000255|PROSITE-
FT ProRule:PRU01202}.
FT NP_BIND 159 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT NP_BIND 697 754 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT REGION 1 401 Carboxyphosphate synthetic domain.
FT REGION 402 546 Oligomerization domain.
FT REGION 547 929 Carbamoyl phosphate synthetic domain.
FT REGION 930 1060 Allosteric domain.
FT METAL 284 284 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 300 300 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 820 820 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 834 834 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ SEQUENCE 1060 AA; 117048 MW; 726655E52ECB3671 CRC64;
MPKRTDIRKI MVIGSGPIVI GQAAEFDYSG TQACLSLKEE GYQVVLVNSN PATIMTDKDI
ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ALSKNGILEE LNVELLGTKL
SAIDKAEDRD LFKQLMEELN QPIPESEIVN SVEEAIQFAE QIGYPLIVRP AFTLGGTGGG
MCDNQEQLVD ITTKGLKLSP VTQCLIERSI AGFKEIEYEV MRDAADNALV VCNMENFDPV
GIHTGDSIVF APAQTLSDVE NQLLRDASLD IIRALKIEGG CNVQLALDPN SFKYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPITK TTYAMFEPAL DYVVAKMPRF
PFDKFESGDR KLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVDHIKIA DLDNVSDDVL
LEKIRKAEDD RLFYLAEALR RHYSIEKLAS LTSIDSFFLD KLRVIVELED LLSKNRLDIN
ILKKVKNKGF SDKAIASLWQ INEDQVRNMR KEAGILPVYK MVDTCASEFD SATPYFYSTY
AVENESLISD KASILVLGSG PIRIGQGVEF DYATVHSVKA IRESGFEAII MNSNPETVST
DFSISDKLYF EPLTFEDVMN VIDLEKPEGV ILQFGGQTAI NLAKDLNKAG VKILGTQLED
LDRAENRKQF EATLQALNIP QPPGFTATTE EEAVNAAQKI GYPVLVRPSY VLGGRAMKIV
ENEEDLRHYM TTAVKASPDH PVLIDAYLIG KECEVDAISD GQNILIPGIM EHIERAGVHS
GDSMAVYPPQ TLSETIIETI VDYTKRLAIG LNCIGMMNIQ FVIKDQKVYV IEVNPRASRT
LPFLSKVTHI PMAQVATKVI LGDKLCNFTY GYDLYPASDM VHIKAPAFSF TKLAKVDSLL
GPEMKSTGEV MGSDINLQKA LYKAFEAAYL HMPDYGNIVF TVDDTDKEEA LELAKVYQSI
GYRIYATQGT AIYFDANGLE TVLVGKLGEN DRNHIPDLIK NGKIQAVINT VGQNNIDNHD
ALIIRRSAIE QGVPLFTSLD TAHAMFKVLE SRAFTLKVLD
//
