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-MAY-2013, entry version 106.
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=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;
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/gen-43-1-116;
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 -!- 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.
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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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; 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; 3.40.50.20; -; 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; CarbamoylP_synth_lsu_oligo; 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; FALSE_NEG.
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.
FT DOMAIN 673 863 ATP-grasp 2.
FT NP_BIND 157 214 ATP (By similarity).
FT NP_BIND 699 756 ATP (By similarity).
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 (By similarity).
FT METAL 296 296 Magnesium or manganese 1 (By similarity).
FT METAL 296 296 Magnesium or manganese 2 (By similarity).
FT METAL 298 298 Magnesium or manganese 2 (By similarity).
FT METAL 822 822 Magnesium or manganese 3 (By similarity).
FT METAL 834 834 Magnesium or manganese 3 (By similarity).
FT METAL 834 834 Magnesium or manganese 4 (By similarity).
FT METAL 836 836 Magnesium or manganese 4 (By similarity).
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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