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CARB_SULIK
ID   CARB_SULIK              Reviewed;        1051 AA.
AC   C4KHM7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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}; OrderedLocusNames=M164_1490;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
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; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC       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 the
CC       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}.
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DR   EMBL; CP001402; ACR42091.1; -; Genomic_DNA.
DR   RefSeq; WP_012735959.1; NC_012726.1.
DR   AlphaFoldDB; C4KHM7; -.
DR   SMR; C4KHM7; -.
DR   EnsemblBacteria; ACR42091; ACR42091; M164_1490.
DR   GeneID; 7939606; -.
DR   KEGG; sid:M164_1490; -.
DR   HOGENOM; CLU_000513_1_3_2; -.
DR   OMA; IEPAGIH; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001479; 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; IPR011607; MGS-like_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; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Repeat.
FT   CHAIN           1..1051
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_1000213881"
FT   DOMAIN          131..325
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          673..863
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          930..1051
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   REGION          1..399
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          400..548
FT                   /note="Oligomerization domain"
FT   REGION          549..930
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          931..1051
FT                   /note="Allosteric domain"
FT   BINDING         157..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         699..756
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         822
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         834
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         834
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         836
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1051 AA;  117896 MW;  09F26D85C79B5E3D 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 SQGNKLLMVG 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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