ID CARB_XANCP Reviewed; 1080 AA.
AC P58943;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 1.
DT 01-MAY-2013, entry version 93.
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=XCC1843;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 /
OS LMG 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(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; AE008922; AAM41132.1; -; Genomic_DNA.
DR RefSeq; NP_637208.1; NC_003902.1.
DR ProteinModelPortal; P58943; -.
DR STRING; 190485.XCC1843; -.
DR PRIDE; P58943; -.
DR EnsemblBacteria; AAM41132; AAM41132; XCC1843.
DR GeneID; 998746; -.
DR KEGG; xcc:XCC1843; -.
DR PATRIC; 24074519; VBIXanCam115730_1967.
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:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
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 GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
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; IPR006195; aa-tRNA-synth_II.
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; Reference proteome;
KW Repeat.
FT CHAIN 1 1080 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145066.
FT DOMAIN 133 328 ATP-grasp 1.
FT DOMAIN 679 876 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 705 762 ATP (By similarity).
FT REGION 1 403 Carboxyphosphate synthetic domain.
FT REGION 404 554 Oligomerization domain.
FT REGION 555 942 Carbamoyl phosphate synthetic domain.
FT REGION 943 1080 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 830 830 Magnesium or manganese 3 (By similarity).
FT METAL 847 847 Magnesium or manganese 3 (By similarity).
FT METAL 847 847 Magnesium or manganese 4 (By similarity).
FT METAL 849 849 Magnesium or manganese 4 (By similarity).
SQ SEQUENCE 1080 AA; 117277 MW; FAD1006D58E54974 CRC64;
MPKRTDLKTI LIIGAGPIVI GQACEFDYSG AQACKALRDE GYRVVLVNSN PATIMTDPNM
ADAVYIEPIN WQTVEKIIAK EKPDALLPTM GGQTALNCAL DLADHGVLEK YNVELIGAKR
EAIRMAEDRE LFRVAMGEIG LDCPRAEVAH TLEEALDIQT RVGYPTIIRP SFTLGGSGGG
IAYNREELID IVGRGLELSP TTEVLVEESV LGWKEFEMEV VRDTADNCII VCAIENLDPM
GVHTGDSITV APAQTLTDKE YQRLRDASIA VLRKIGVDTG GSNVQFGISP TTGRVVVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELKNEIT GGLTPASFEP SIDYVVTKIP
RFAFEKFPQA DARLTTQMKS VGEVMAMGRT FQESLQKALR GLETGKIGLD PTGLDLGSED
DMAALKRELK APGPERLFYV GDAFRAGMSV ADVYALSFID PWFLDQIEEL ISLEQQLADD
GMAALDAPRL RLLKRAGFSD ARLAELIGTN EEAVRTLRRA LKVRPVYKRV DSCAAEFATS
TAYLYSTYED ECEALPSNRD KIMILGGGPN RIGQGIEFDY CCVHAALALR DDGFETIMVN
CNPETVSTDY DTSDRLYFEP LTLEDVLEIV ELEQPKGVIV QYGGQTPLKL ARALEANGVP
VIGTSPDSID LAEDRERFQQ LVDKLGLKQP PNRIARNADE ALVLAREIGY PLVVRPSYVL
GGRAMEIVYG ESDLARYVRD AVKVSNDSPV LLDRFLDNAV EVDVDIIADK DGNVLIGGVM
EHIEEAGVHS GDSSCSLPPY SLSAETQAEL RRQVVMLAEG LNVVGLMNTQ FAVQVNDAGD
DIVYLLEVNP RASRTVPFVS KATGMPLAKI AARCMAGKTL AEQGATKEIV PDYYSVKEAI
FPFAKFQGVD PILGPEMRST GEVMGVGRSF GAAFARAQEA GGIKAPPLGK AFVSVRDPDK
QRVLPVAQAL VERGFTLVAT RGTGAWLQQH GLSCEIVNKV AEGRPHIVDS IKNGEIVYIV
NTTEGRAAIS DSFSIRREAL QHRVTYSTTV AGAKALVHSL EFRGTGPVWS LQELHKELEA
//
