CARB_DEIRA
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 03-AUG-2022, entry version 140.
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=DR_0668;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC 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 / NCIMB
RC 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 radiodurans
RT 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; 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; 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 AlphaFoldDB; Q9RWK0; -.
DR SMR; Q9RWK0; -.
DR STRING; 243230.DR_0668; -.
DR PRIDE; Q9RWK0; -.
DR EnsemblBacteria; AAF10248; AAF10248; DR_0668.
DR KEGG; dra:DR_0668; -.
DR PATRIC; fig|243230.17.peg.845; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_0; -.
DR InParanoid; Q9RWK0; -.
DR OMA; IEPAGIH; -.
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: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 GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; 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; 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; 2.
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; Reference proteome; Repeat.
FT CHAIN 1..1024
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145003"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 671..863
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 930..1024
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..402
FT /note="Carboxyphosphate synthetic domain"
FT REGION 403..546
FT /note="Oligomerization domain"
FT REGION 547..929
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 930..1024
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 697..755
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 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
