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Database: UniProt
Entry: Q8U085
LinkDB: Q8U085
Original site: Q8U085 
ID   CARB_PYRFU              Reviewed;        1056 AA.
AC   Q8U085;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JAN-2019, entry version 114.
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=PF1714;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
RT   P. horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81838.1; -; Genomic_DNA.
DR   RefSeq; WP_011012860.1; NC_003413.1.
DR   ProteinModelPortal; Q8U085; -.
DR   SMR; Q8U085; -.
DR   STRING; 186497.PF1714; -.
DR   PRIDE; Q8U085; -.
DR   EnsemblBacteria; AAL81838; AAL81838; PF1714.
DR   GeneID; 1469591; -.
DR   KEGG; pfu:PF1714; -.
DR   PATRIC; fig|186497.12.peg.1782; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 911at2157; -.
DR   BioCyc; PFUR186497:G1FZR-1770-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001013; 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   Gene3D; 3.40.50.1380; -; 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; IPR036914; MGS-like_dom_sf.
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   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 1.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1056       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145082.
FT   DOMAIN      131    325       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      661    849       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      915   1043       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     157    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     687    744       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    536       Oligomerization domain.
FT   REGION      537    919       Carbamoyl phosphate synthetic domain.
FT   REGION      920   1056       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       809    809       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       820    820       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       820    820       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       822    822       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1056 AA;  118057 MW;  631BAA3D3C5C21A7 CRC64;
     MKIDVSKVIV IGSGAIKIGE AAEFDYSGSQ ALKALREEGI ESVLVNPNVA TIQTSYELAD
     KVYLLPLKTE FIEKVIEKEK PDGILVGFGG QTALSLGVSL YKKGILDKYN VKVLGTPIEG
     IERALDREKF QKTMKKVGLP VPPSDAAKTP EEAIEIAESI GFPVIVRVSF NLGGRGSFIA
     RSREEFEKYI IRAFAQSEIR KVLVEKYLNG WKEIEFEVVR DKAGNSVAVV CLENVDPMGV
     HTGESIVVGP SQTLTNREYQ MLRDAAIRVA DAIELIGEGN VQLALSPNSE EYYVIETNPR
     MSRSSALASK VTGYPLAYIA TKLAIGYTLD ELRNTVTGIT TAAFEPSLDY VAVKIPRWDF
     KKFEEVNKSI GSEMKSIGEV MAIGRNLHEA FQKAIRMLDI GDELIGKYYL EDEPLENVLE
     RLKKKEPYLL MHIAKALRLG ATVEDIHKIT KVDKFFIYVI EDLVKIAEEL RKNPTEELIR
     EAKRLGFSDW EIELLTKRKV KKKWKPVVKN IDTLAGEFPA KTNYLYVTYD GVENDIPKPK
     KPSILVLGAG VFRIGVSVEF DWAVVNFVNA IRKRGIEAAI LNYNPETVST DWDMSDRLYF
     EEITLERVLD IYEFERPIGV VAFAGGQLAN SLAKKLENAG VKLLGTSGKS VDKAENRAKF
     SKLLEKLGIP QPEWISAESI DEAIKLAKKI EYPVIVRPSY VLSGTAMKVA WNEKELIDFL
     KEAASVSPEH PVLISKFIPG TEAEIDAVSD GKKVVGVTLE HIEGAGVHSG DSTMVTPWRT
     LSERNVKRIW EITYELAKEL EIKGPFNVQF VIDKKPYVLE LNLRTSRSMP FSSKSRGVNL
     MELSAQAVLD GELKIGVEGK YYEIPPVAYG VKSPQFSWAQ LQGAYPFLGP EMRSTGEVAA
     LGTHYEDALL KSWLSVKPNE LPKTSALIYG WEKKNILKET AKILENLGIT TYSIGGDIGE
     INISKQEAVN MIKEGKIDII MTTGYAKDKD YEIRRLAADL NVPLVLDANL ALELAKAIEW
     KTKTQEEFEI KELREYWIRK IEENVEEYAA SVVLRR
//
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