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Database: UniProt
Entry: Q9RWK0
LinkDB: Q9RWK0
Original site: Q9RWK0 
ID   CARB_DEIRA              Reviewed;        1024 AA.
AC   Q9RWK0;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 130.
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=DR_0668;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(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; AE000513; AAF10248.1; -; Genomic_DNA.
DR   PIR; F75489; F75489.
DR   RefSeq; NP_294391.1; NC_001263.1.
DR   RefSeq; WP_010887313.1; NZ_CP015081.1.
DR   ProteinModelPortal; Q9RWK0; -.
DR   SMR; Q9RWK0; -.
DR   STRING; 243230.DR_0668; -.
DR   PRIDE; Q9RWK0; -.
DR   EnsemblBacteria; AAF10248; AAF10248; DR_0668.
DR   GeneID; 1800093; -.
DR   KEGG; dra:DR_0668; -.
DR   PATRIC; fig|243230.17.peg.845; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   InParanoid; Q9RWK0; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IBA:GO_Central.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; 2.
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   1024       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145003.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      671    863       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      930   1024       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     697    755       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    546       Oligomerization domain.
FT   REGION      547    929       Carbamoyl phosphate synthetic domain.
FT   REGION      930   1024       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       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   1024 AA;  111647 MW;  A7CAB7A99C6B9715 CRC64;
     MPKRTDLQTI LILGSGPIQI GQAAEFDYSG TQALKALKNE GYRVILVNSN PATIMTDPEL
     ADATYLEPLT PEFVEKIIEK EKPDAILPTL GGQTALNLAM ELHERGSLEK YGVELIGAGV
     EAIKKGEDRE LFQAAMKKIG VETARGKMVH SMEEAVEYQK EIGLPIVIRP SFTLGGTGGG
     IAHTYEEFLA ITEGGLRDSP VTSVLLEESI LGWKEYELEV MRDTADTVII ITSIENFDPM
     GVHTGDSITV APAQTLSDVE YQRLRDQSLA IIREIGVATG GSNIQFAVNP DNGRVIVIEM
     NPRVSRSSAL ASKATGFPIA KIAALLAVGY HLDELPNDIT RVTPASFEPS IDYVVTKIPR
     FAFEKFPGTP DGLGTQMRSV GEVMAIGRTF KESLQKALRS TEGDIRGVYA EMDEAGLRAL
     LYPNPRRIEA VIELLRRGES VESLFDATKI DRWFLSQLKE IMDAEKEILD LGPIAEWKYE
     LWREVKRLGF SDARIGEIVG LSELEVRDLR KKAKATPVYK TVDTCAAEFE AHTPYHYSTY
     EWEDEVAPTD KPKVVILGSG PNRIGQGVEF DYATVHAVWA LQEAGYETIM VNSNPETVST
     DYDTADRLYF EPLTFEDVMN IVEHEKPVGV IVQLGGQTPL KLAKKLADAG APIIGTSPET
     IHEAEDRASF NALCERLGLP QPRGKVAQTP AQARELAAEL GFPLMARPSY VLGGRAMRTV
     RSMDELTTYL DEVYAAVEGQ PSILLDQFLE GALELDVDTL CDGERAVVAG IMEHVEAAGV
     HSGDSACILP PVTLDAGVLE RVKADTERLA LELGVRGLMN VQWAVKDGTA YILEANPRAS
     RTVPFVSKAV NHPLAKSAAR IAAGQTLEQI GLLETPTPRM YSVKEVHLPF LKFKDVLPVL
     GPEMKSTGES MGIDSDPYLA FYRAQLGAKN YLPLEGTALL IGDGLDEVAG TLEGAGLKVI
     REQDGDELPD LLIDVTGSPL LRTALERGVP IVSTKEGAEW TARAVAEAKK AGMLGVRSLQ
     EWVK
//
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