GenomeNet

Database: UniProt
Entry: Q8E5F5
LinkDB: Q8E5F5
Original site: Q8E5F5 
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
//
DBGET integrated database retrieval system