ID CARB_RALSO Reviewed; 1081 AA.
AC Q8XZ83;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 01-MAY-2013, entry version 88.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; OrderedLocusNames=RSc1521; ORFNames=RS03783;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S.,
RA Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L.,
RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N.,
RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T.,
RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M.,
RA Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (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
CC the large (or ammonia) chain to synthesize carbamoyl phosphate (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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DR EMBL; AL646052; CAD15223.1; -; Genomic_DNA.
DR RefSeq; NP_519642.1; NC_003295.1.
DR ProteinModelPortal; Q8XZ83; -.
DR STRING; 267608.RSc1521; -.
DR PRIDE; Q8XZ83; -.
DR EnsemblBacteria; CAD15223; CAD15223; RSc1521.
DR GeneID; 1220350; -.
DR KEGG; rso:RSc1521; -.
DR PATRIC; 20261693; VBIRalSol70888_1556.
DR eggNOG; COG0458; -.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; SEFFEIV; -.
DR ProtClustDB; PRK05294; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 2.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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.
DR Pfam; PF00289; CPSase_L_chain; 2.
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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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.
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 1081 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145031.
FT DOMAIN 133 335 ATP-grasp 1.
FT DOMAIN 683 878 ATP-grasp 2.
FT NP_BIND 166 223 ATP (By similarity).
FT NP_BIND 709 766 ATP (By similarity).
FT REGION 1 410 Carboxyphosphate synthetic domain.
FT REGION 411 558 Oligomerization domain.
FT REGION 559 944 Carbamoyl phosphate synthetic domain.
FT REGION 945 1081 Allosteric domain.
FT METAL 292 292 Magnesium or manganese 1 (By similarity).
FT METAL 306 306 Magnesium or manganese 1 (By similarity).
FT METAL 306 306 Magnesium or manganese 2 (By similarity).
FT METAL 308 308 Magnesium or manganese 2 (By similarity).
FT METAL 833 833 Magnesium or manganese 3 (By similarity).
FT METAL 849 849 Magnesium or manganese 3 (By similarity).
FT METAL 849 849 Magnesium or manganese 4 (By similarity).
FT METAL 851 851 Magnesium or manganese 4 (By similarity).
SQ SEQUENCE 1081 AA; 117896 MW; F6BF743D810AAF68 CRC64;
MPKRTDIKTI LIIGAGPIII GQACEFDYSG AQACKALREE GFKVVLVNSN PATIMTDPST
ADVTYIEPIT WEVVERIIAK ERPDAILPTM GGQTALNCAL DLHRHGVLEK YNVELIGASP
EAIDKAEDRQ KFKEAMTKIG LGSAKSGIAH SLEEALAVQA QIARETSSGG YPIVIRPSFT
LGGTGGGIAY NREEFEDICK RGLDLSPTNE LLIEESLLGW KEYEMEVVRD KKDNCIIVCS
IENLDPMGIH TGDSITVAPA QTLTDKEYQI LRNASLAVLR EIGVDTGGSN VQFSINPEDG
RMIVIEMNPR VSRSSALASK ATGFPIAKVA AKLAVGYTLD ELKNEITGGA TPASFEPSID
YVVTKVPRFA FEKFPQADSH LTTQMKSVGE VMAMGRTFQE SFQKALRGLE VGVDGLDEKS
SDRDEIIAEI GEPGPDRIWY LGDAFRLGLS IDEVYAETAV DPWFLAQIED IVRTEALVKA
RTLDSLSAAE LRLLKQKGFS DRRLATLMKT TAQAVREKRI AEKVRPVYKR VDTCAAEFAT
NTAYLYSTYE AEHGECEADP TERKKIMVLG GGPNRIGQGI EFDYCCVHAA LALREDGYET
IMVNCNPETV STDYDTSDRL YFEPVTLEDV LEIVDKEKPV GVIVQYGGQT PLKLALDLEA
NGVPIIGTTP DMIDAAEDRE RFQKLLHDLG LRQPPNRTAR AEDEALKLAD EIGYPLVVRP
SYVLGGRAME IVHEPRDLER YMREAVKVSN DSPVLLDRFL NDAIECDVDC LSDGKRVFIG
GVMEHIEQAG VHSGDSACSL PPYSLSQATV DELKRQTAAM ARALNVIGLM NVQFAIQQKG
GEDIVYVLEV NPRASRTVPY VSKATGISLA KVAARCMAGQ SLDEQGIHDE VVPSYYSVKE
AVFPFNKFPG VDPVLGPEMR STGEVMGVGR TFGEALFKSQ LAAGSRLPEK GTVLMTVKDS
DKPRAIEVAR TLHTLGYPIV ATRGTASAIE AAGIPVRVVN KVKDGRPHIV DMIKNGELAL
VFTTVDETRA AIADSRSIRT AALANRVTYY TTIAGARAAV EGLKHLQNLD VYDLQGLHAS
L
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