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-MAY-2013, entry version 89.
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=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 -!- 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; 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; PMANLAT; -.
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; 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; Repeat.
FT CHAIN 1 1068 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145027.
FT DOMAIN 133 328 ATP-grasp 1.
FT DOMAIN 673 864 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 699 756 ATP (By similarity).
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 (By similarity).
FT METAL 299 299 Magnesium or manganese 1 (By similarity).
FT METAL 299 299 Magnesium or manganese 2 (By similarity).
FT METAL 301 301 Magnesium or manganese 2 (By similarity).
FT METAL 823 823 Magnesium or manganese 3 (By similarity).
FT METAL 835 835 Magnesium or manganese 3 (By similarity).
FT METAL 835 835 Magnesium or manganese 4 (By similarity).
FT METAL 837 837 Magnesium or manganese 4 (By similarity).
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
//
