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Database: UniProt
Entry: C3N664
LinkDB: C3N664
Original site: C3N664 
ID   CARB_SULIA              Reviewed;        1051 AA.
AC   C3N664;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   26-NOV-2014, entry version 37.
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=M1627_1608;
OS   Sulfolobus islandicus (strain M.16.27).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.27;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {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; CP001401; ACP55489.1; -; Genomic_DNA.
DR   RefSeq; YP_002843534.1; NC_012632.1.
DR   ProteinModelPortal; C3N664; -.
DR   STRING; 427318.M1627_1608; -.
DR   EnsemblBacteria; ACP55489; ACP55489; M1627_1608.
DR   GeneID; 7814542; -.
DR   KEGG; sim:M1627_1608; -.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; GSDRIWY; -.
DR   BioCyc; SISL427318:GH3D-1667-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; Repeat.
FT   CHAIN         1   1051       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000213880.
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;  117878 MW;  FEEE1C42DBEB1104 CRC64;
     MKETPKKVLV IGSGPIKIAE AAEFDYSGSQ ALKALKEEGI ETVLVNSNVA TVQTSKKFAD
     KLYMLPVVWW AVEKVIEKER PDGIMIGFGG QTALNVGVDL HKKGVLQKYG VKVLGTQIDG
     IEKALSREKF RETMIENNLP VPPSLSARSE EEAIKNAKIV GYPVMVRVSF NLGGRGSMVA
     WTEEDLKKNI RRALSQSYIG EVLIEKYLYH WIELEYEVMR DKKGNSAVIA CIENLDPMGV
     HTGESTVVAP CQTLDNLEYQ NMRTYTIEVA RSINLIGECN VQFALNPRGY EYYIIETNPR
     MSRSSALASK ATGYPLAYVS AKLALGYELH EVINKVSGRT CACFEPSLDY IVTKIPRWDL
     SKFENVDQSL ATEMMSVGEV MSIGRSFEES LQKAVRMLDI GEPGVVGGKI YEAKMSKVEA
     LKYLKERRPY WFLYVAKAFK EGATIDEVYE VTGISKFFLN KIKGLVDFYE TLKILKEIDE
     ETLKLAKKLG FSDEQISKAL NKSTEYVRKI RDQSNIIPVV KLIDTLAGEW PSVTNYMYLT
     YNGTEDDLEF SQGNKLLIVG AGGFRIGVSV EFDWSVVSLM EAASKYFDEV AVLNYNPETV
     STDWDIARKL YFDEINVERV LDLIKKEKFR YVATFSGGQI GNSIAKELEE NGVRLLGTSG
     SSVDIAENRE KFSKLLDKLG ISQPNWVSAT SLEEIKKFVN EVGFPVLVRP SYVLSGSSMK
     IAYSEEELYE YVRRATEISP KYPVVISKYI ENAIEAEVDG VSDGNRVLGI TLEHVEEAGV
     HSGDATMSIP FRKLSENSVN KMRENVLSLA RELNIKGPFN VQFVVKDNTP HIIELNLRAS
     RSMPFSSKAK GINLINESMK AIFNGLDFSE DYYEPPSKYW AVKSPQFSWS QLRGTYPFLG
     PEMKSTGEAA SFGVTFYDAL LKSWLSSIPN RIPNKNGIAL VYGDKNLDYL KDTAVNLVKF
     GLTVYSISEL PLQGIETIDK TKAEELVRAK KVEIVVTDGY LKKFDYNIRR TAVDYNIPVI
     LNGRLGYEVS KAFLDYDSLT FFEISEYGGG I
//
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