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Database: UniProt
Entry: Q9ZB63
LinkDB: Q9ZB63
Original site: Q9ZB63 
ID   CARY_GEOSE              Reviewed;        1043 AA.
AC   Q9ZB63;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   05-DEC-2018, entry version 89.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=carB;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12980 / DSM 22 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC
RC   10339 / VKM B-510;
RX   PubMed=9370352; DOI=10.1111/j.1432-1033.1997.00443.x;
RA   Yang H., Park S.M., Nolan W.G., Lu C.-D., Abdelal A.T.;
RT   "Cloning and characterization of the arginine-specific carbamoyl-
RT   phosphate synthetase from Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 249:443-449(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Abdelal A.T.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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;
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable up to 63 degrees Celsius.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
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   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
DR   EMBL; U43091; AAC78719.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9ZB63; -.
DR   SMR; Q9ZB63; -.
DR   PRIDE; Q9ZB63; -.
DR   SABIO-RK; Q9ZB63; -.
DR   UniPathway; UPA00068; UER00171.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 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; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding; Repeat.
FT   CHAIN         1   1043       Carbamoyl-phosphate synthase arginine-
FT                                specific large chain.
FT                                /FTId=PRO_0000144990.
FT   DOMAIN      134    328       ATP-grasp 1.
FT   DOMAIN      676    863       ATP-grasp 2.
FT   DOMAIN      930   1037       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     160    217       ATP. {ECO:0000250}.
FT   NP_BIND     702    756       ATP. {ECO:0000250}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    550       Oligomerization domain.
FT   REGION      551    932       Carbamoyl phosphate synthetic domain.
FT   REGION      933   1043       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       299    299       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       299    299       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       301    301       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       822    822       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       834    834       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       834    834       Magnesium or manganese 4. {ECO:0000250}.
FT   METAL       836    836       Magnesium or manganese 4. {ECO:0000250}.
SQ   SEQUENCE   1043 AA;  114522 MW;  E97E7334E70B4C11 CRC64;
     MPKDSSLQSI LLIGSGRSSS AKAAEFDYSG TQACIAFKEE GYRVILVNNN PATIMTDDVH
     ADAVYFEPLT VEAVEAIIAK ETPDGLLATF GGQTGLNLAF QLHEAGVLKK YGVRLLGTPI
     EAIKRPRGGP RTFRALMHEL GEPVPESEIV TSVEEAVAFA EQIGFPIIIR PAYTLGGTGG
     GIAENMEQFL ALVEKGLNES PIHQCLIERS VAGFKEIEYE VMRDQSNTCI TVCNMENVDP
     VGIHTGDSIV VAPSQTLTDE EYQMLRSSAV KIISALGIIG GCNIQFALDP NSKQYYLIEV
     NPRVSRSSAL ASKATGYPIA ALPAKLAVGY TLAELVNPVT KTTYASFEPA LDYVVVKFPR
     LPFDKFPHAD RKLGTQMKAT GEVMAIDRNM ERAFQKAVQS LEGKNNGLLL PELSVKTNDE
     LKQLLVDKDD RRFFAILELL RRGVAVEAIH KWTKIDRFFL CSFERLVALE KQAAAATLDT
     IEEQTFRFLK EKGCSDAFLA ETWGVTELDV RNKRKELGIV PSYKMVDTCA AEFHSETDYY
     YSTYFGEDER KQPSGKEKVL IIGAGPIRIG QGIEFDYSSV HSVFALQKEG YETVMINNNP
     ETVSTDFAVA DRLYFEPLTL ESVLDVIEAE QIKHVIVQFG GQTAINLVKG LEEAGVPLLG
     VTYDMIDQLE DRDRFYQLLE ELDIPHVPGL VANNAEELAA KAAEIGYPVL LRPSYVIGGC
     GMFIVHSEAQ LAALIEQGEL TYPILIDAYL DGKEAEADIV TDGTDIVLPV IIEHVEKAGV
     HSGDSYAWLP AQTLTGEEKA KIIDYAGRIA KKLGFKGIMN IQYVIADGNV YVLEVNPRAS
     RTVPIVSKTT GVPLAQIATK LLLGKSLVDI VDEKARGLAV MPYAVLKYPV FSTHKLPGVD
     PMVGPEMKST GEGISIAATK EEAAYKAFYP YLQKKANANE VYVIGNIDAE LEAEMTAKQL
     TIVADVPFSD WVKRDTALAV IDLGKEEGEA NKRMTALSRQ LLVFTERETL KLFLQALDVD
     HLDVQPIHGW LEKKKQAEQA VIA
//
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