ID CARB_SULIL Reviewed; 1051 AA.
AC C3MQE3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 16-JAN-2019, entry version 62.
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=LS215_1601;
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1;
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:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC 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}.
DR EMBL; CP001399; ACP35606.1; -; Genomic_DNA.
DR RefSeq; WP_012713783.1; NC_012589.1.
DR ProteinModelPortal; C3MQE3; -.
DR SMR; C3MQE3; -.
DR EnsemblBacteria; ACP35606; ACP35606; LS215_1601.
DR GeneID; 7807980; -.
DR KEGG; sis:LS215_1601; -.
DR HOGENOM; HOG000234583; -.
DR KO; K01955; -.
DR OMA; AVFPFNK; -.
DR OrthoDB; 911at2157; -.
DR BioCyc; SISL429572:G1GUX-1635-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001747; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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.
DR PROSITE; PS51855; MGS; 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_1000213882.
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 DOMAIN 930 1051 MGS-like. {ECO:0000255|PROSITE-
FT ProRule:PRU01202}.
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; 117877 MW; 970E75BFE17055A3 CRC64;
MKETPKKVLV IGSGPIKIAE AAEFDYSGSQ ALKALKEEGI ETVLVNSNVA TVQTSKKFAD
KLYMLPVVWW AVEKVIEKER PDGIMIGFGG QTALNVGVDL HKKGVLQKYG VKVLGTQIDG
IEKALSREKF RETMIENNLP VPPSLSARSE EEAIKNAKIV GYPVMVRVSF NLGGRGSMVA
WTEEDLKKNI RRALSQSYIG EVLIEKYLYH WIELEYEVMR DKKGNSSVIA 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 NKSTQYVRKI 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 GINLINEAMK AIFNGLDFSE DYYEPPSKYW AVKSPQFSWS QLRGTYPFLG
PEMKSTGEAA SFGVTFYDAL LKSWLSSIPN RIPNKNGIAL VYGDKNLDYL KDTAVNLVKF
GLTVYSISEL PLQGIETIDK TKAEELVRAK KVEIVVTDGY LKKFDYNIRR TAVDYNIPVI
LNGRLGYEVS KAFLDYDSLT FFEISEYGGG I
//
