CARY_GEOSE
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 03-AUG-2022, entry version 97.
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 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / 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-phosphate
RT 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; carbamoyl
CC 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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; U43091; AAC78719.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZB63; -.
DR SMR; 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; 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; 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
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000144990"
FT DOMAIN 134..328
FT /note="ATP-grasp 1"
FT DOMAIN 676..863
FT /note="ATP-grasp 2"
FT DOMAIN 930..1037
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..402
FT /note="Carboxyphosphate synthetic domain"
FT REGION 403..550
FT /note="Oligomerization domain"
FT REGION 551..932
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 933..1043
FT /note="Allosteric domain"
FT BINDING 160..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 702..756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="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
