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Database: UniProt
Entry: Q59969
LinkDB: Q59969
Original site: Q59969 
ID   CARB_SULSO              Reviewed;        1051 AA.
AC   Q59969;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   01-OCT-2014, entry version 112.
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=SSO0641;
OS   Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
OS   P2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8752005; DOI=10.1093/oxfordjournals.molbev.a025665;
RA   Lawson F.S., Charlebois R.L., Dillon J.A.;
RT   "Phylogenetic analysis of carbamoylphosphate synthetase genes: complex
RT   evolutionary history includes an internal duplication within a gene
RT   which can root the tree of life.";
RL   Mol. Biol. Evol. 13:970-977(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D.,
RA   Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C.,
RA   Kushwaha N., Lafleur E., Medina N., Peng X., Penny S.L., She Q.,
RA   St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F.,
RA   Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of
RT   the extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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   -!- 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; U33768; AAA99059.1; -; Genomic_DNA.
DR   EMBL; Y18930; CAB57658.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40949.1; -; Genomic_DNA.
DR   PIR; T43253; T43253.
DR   RefSeq; NP_342159.1; NC_002754.1.
DR   ProteinModelPortal; Q59969; -.
DR   STRING; 273057.SSO0641; -.
DR   EnsemblBacteria; AAK40949; AAK40949; SSO0641.
DR   GeneID; 1454916; -.
DR   KEGG; sso:SSO0641; -.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; KNPTHER; -.
DR   BioCyc; SSOL273057:GCH2-611-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 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; 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   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00867; CPSASE_2; 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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1051       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145084.
FT   DOMAIN      131    325       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      673    863       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     157    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     699    756       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    548       Oligomerization domain.
FT   REGION      549    930       Carbamoyl phosphate synthetic domain.
FT   REGION      931   1051       Allosteric domain.
FT   METAL       282    282       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       296    296       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       296    296       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       298    298       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       822    822       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       834    834       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       834    834       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       836    836       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1051 AA;  118204 MW;  07FE2415283B799D CRC64;
     MRETPKKVLV IGSGPIKIAE AAEFDYSGSQ ALKALKEEGI ETVLVNSNVA TVQTSKKFAD
     KLYMLPVVWW AVEKVIEKER PDGIMIGFGG QTALNVGVDL HKKGVLQKYN VKVLGTQIDG
     IEKALSREKF RETMIENNLP VPPSLSARSE EEAIKNAKIV GYPVMVRVSF NLGGRGSMVA
     WTEEDLKKNI RRALSQSYIG EVLLEKYLYH WIELEYEVMR DKKGNSAVIA CIENLDPMGV
     HTGESTVVAP CQTLDNLEYQ NMRTYTIEVA RSINLIGECN VQFALNPRGY EYYIIETNPR
     MSRSSALASK ATGYPLAYVS AKLALGYELH EVINKVSGRT CACFEPSLDY IVTKIPRWDL
     SKFENVDQSL ATEMMSVGEV MSIGRSFEES LQKAIRMLDI GEPGVVGGKV YESNMSKEEA
     LKYLKERRPY WFLYAAKAFK EGATINEVYE VTGINEFFLN KIKGLVDFYE TLRKLKEIDK
     ETLKLAKKLG FSDEQISKAL NKSTEYVRKI RYETNTIPVV KLIDTLAGEW PAVTNYMYLT
     YNGTEDDIEF SQGNKLLIIG AGGFRIGVSV EFDWSVVSLM EAGSKYFDEV AVLNYNPETV
     STDWDIARKL YFDEISVERV LDLIKKEKFR YVATFSGGQI GNSIAKELEE NGVRLLGTSG
     SSVDIAENRE KFSKLLDKLG ISQPDWISAT SLGEIKKFAN EVGFPVLVRP SYVLSGSSMK
     IAYSEEELYE YVRRATEISP KYPVVISKYI ENAIEAEIDG VSDGNKVLGI TLEHIEEAGV
     HSGDATMSIP FRKLSENNVN RMRENVLNIA RELNIKGPFN VQFVVKENTP YIIELNLRAS
     RSMPFSSKAK GINLINESMK AIFDGLDFSE DYYEPPSKYW AVKSAQFSWS QLRGAYPFLG
     PEMKSTGEAA SFGVTFYDAL LKSWLSSMPN RIPNKNGIAL VYGNKNLDYL KDTADNLTRF
     GLTVYSISEL PLQDIETIDK MKAEELVRAK KVEIIVTDGY LKKFDYNIRR TAVDYNIPII
     LNGRLGYEVS KAFLNYDSLT FFEISEYGGG I
//
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