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
//
