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Database: UniProt
Entry: Q9CKV0
LinkDB: Q9CKV0
Original site: Q9CKV0 
ID   CARB_PASMU              Reviewed;        1068 AA.
AC   Q9CKV0;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   01-OCT-2014, entry version 95.
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=PM1505;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit.
CC       {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}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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DR   EMBL; AE004439; AAK03589.1; -; Genomic_DNA.
DR   RefSeq; NP_246444.1; NC_002663.1.
DR   ProteinModelPortal; Q9CKV0; -.
DR   STRING; 272843.PM1505; -.
DR   PRIDE; Q9CKV0; -.
DR   EnsemblBacteria; AAK03589; AAK03589; PM1505.
DR   GeneID; 1244852; -.
DR   KEGG; pmu:PM1505; -.
DR   PATRIC; 22872287; VBIPasMul88067_1521.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; GSDRIWY; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; PMUL272843:GC8W-1563-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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-UniPathway.
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_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; 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; 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; 1.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1068       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145027.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      673    864       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     699    756       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT   REGION      404    548       Oligomerization domain.
FT   REGION      549    930       Carbamoyl phosphate synthetic domain.
FT   REGION      931   1068       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       823    823       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       837    837       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1068 AA;  117232 MW;  759B46E0FBC1A56E CRC64;
     MPKRTDINTI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVVLVNSN PATIMTDPDM
     ADVTYIEPIE WRTVEKIIEK ERPDAILPTM GGQTALNCAL DLSKNGVLKK YNVELIGAKE
     DAIDKAEDRG RFKEAMEKIG LSTPKSFVCH TLEEAWAAQS EVGFPTLIRP SFTMGGSGGG
     IAYNKDEFYA ICERGFDASP THELLIEQSV LGWKEYEMEV VRDKADNCII VCSIENFDPM
     GVHTGDSITV APAQTLTDKE YQIMRNASIA VLREIGVDTG GSNVQFAINP ENGEMIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLNELRNDIT GGLIPASFEP SIDYVVTKVP
     RFAFEKFPQA DDRLTTQMKS VGEVMAMGRT FQESLQKALR GLETGICGFN LMSEEPEKIR
     QELGNPGPIR ILYVADAFGA GFTLDEVHHY SKIDPWFLIQ IQDLVLEELA LEKRTLDDLD
     YAELRRLKRK GFSDKRIAQL TKSAESAVRN KRVSLNLHPV YKRVDTCAGE FTSDTAYLYS
     TYEEECESRP SDKKKIMILG GGPNRIGQGI EFDYCCVHAS LALREAGFET IMVNCNPETV
     STDFDTSDRL YFEPLTLEDV LEIIHVEKPH GVIVHYGGQT PLKLANDLHA NGVNIIGTSA
     DSIDAAEDRE RFQQILHKLH LKQPTNRTAR NAEEAVKLAE EVGYPLVVRP SYVLGGRAMQ
     IVYNVDELQR YMREAVSVSN DSPILLDHFL NNAIEVDVDC ICDGAEVVIG GIMQHIEQAG
     IHSGDSACSL PPYSLSQEVQ DEIRRQTAEM AFALGVKGLM NVQFAVQDGV IYVLEVNPRA
     SRTVPFVSKA TGRPLAKIAA RVMAGESLKA QGIQGEVIPP FYSVKEAVFP FIKFPGVDTV
     LGPEMRSTGE VMGVGTTFAE AFLKAQLGAN ERIPKTGKVF LSVNDADKPR LLPIARQLQE
     SGYGLCATLG TAKFLREHGV AVQIINKVRE GRPNIVDAIK NGEIAMVINT VSGLAETVTD
     GHAIRRSALQ QKVFLQTTLA GAEALAGSVE YLADSEVYSL QDLHQRLL
//
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