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Database: UniProt
Entry: Q9K8V7
LinkDB: Q9K8V7
Original site: Q9K8V7 
ID   CARY_BACHD              Reviewed;        1047 AA.
AC   Q9K8V7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 116.
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; OrderedLocusNames=BH2895;
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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   -!- 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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
DR   EMBL; BA000004; BAB06614.1; -; Genomic_DNA.
DR   PIR; G84011; G84011.
DR   RefSeq; WP_010899042.1; NC_002570.2.
DR   ProteinModelPortal; Q9K8V7; -.
DR   SMR; Q9K8V7; -.
DR   STRING; 272558.BH2895; -.
DR   EnsemblBacteria; BAB06614; BAB06614; BAB06614.
DR   KEGG; bha:BH2895; -.
DR   eggNOG; ENOG4108K60; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; FADEIYF; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; BHAL272558:G1G3A-2972-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000001258; Chromosome.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN         1   1047       Carbamoyl-phosphate synthase arginine-
FT                                specific large chain.
FT                                /FTId=PRO_0000144988.
FT   DOMAIN      133    327       ATP-grasp 1.
FT   DOMAIN      676    865       ATP-grasp 2.
FT   DOMAIN      937   1047       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000250}.
FT   NP_BIND     702    758       ATP. {ECO:0000250}.
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    549       Oligomerization domain.
FT   REGION      550    933       Carbamoyl phosphate synthetic domain.
FT   REGION      934   1047       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       298    298       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       298    298       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       300    300       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       824    824       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       836    836       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       836    836       Magnesium or manganese 4. {ECO:0000250}.
FT   METAL       838    838       Magnesium or manganese 4. {ECO:0000250}.
SQ   SEQUENCE   1047 AA;  115860 MW;  1AAA7676D583A311 CRC64;
     MPKRTDIQSV LVIGSGPIVI GQAAEFDYAG AQACLALREE GIQVILVNNN PATVMTDEAC
     ADVVYFEPLT VASVKNIIER ERPDGLLATL GGQTGLNLAM KLEEAGILEA YNVELLGTPM
     ESIKKGEDRE AFRQLMHELH EPVPESEIVH SVAEAVDFAN TVGYPIIVRP AYTLGGAGGG
     IAESEEALIR IVKGGLELSP IQQCLIEKSI AGFKEIEYEV MRDSNDTCIT VCNMENIDPV
     GVHTGDSIVV APSQTLTDQE YQMLRSASLK IIRTLGIVGG CNIQFALDPD SKQYYLIEVN
     PRVSRSSALA SKATGYPIAR MAAKLSLGYG LHELKNPVTE DTYASFEPSL DYVVVKFPRW
     PFDKLVHVNR ELGTQMKATG EVMAIERNLE AGLQKAVRSL EIKTHGLSLP SLSQWEDSEL
     WVIVKKADDR RFFAILELLR RGVTIEAIHE QTKIDRFFLT SFAKLMTLEK EIAGQSLDDI
     TSDELSTYKK YGFSDEWLAS SWGVGLADVR HTRKALGVVP SYKMVDTCAA EFEAKTPYYY
     SSWTGENDLL LPEKAKERVL IIGSGPIRIG QGIEFDYCSV HGAKSLRARN FEAIIINNNP
     ETVSTDYETA DRLYFEPLAV EDVLNVIEVE NVDHVIVQLG GQTAIGLTKG LEEAGVSILG
     TTQDVIDQLE DRERFYEFMR SVEVPHIPGK TAETKEELLK AAQSIGYPIL LRPSYVIGGQ
     GMFIASNQEE LAAFCEDKNH SVTFPILVDA YYPGVEFEVD VLTDGSDIFI PGMFEHVEKA
     GVHSGDSMAV TPPPTLEAKW KQQAINYTRQ IAKGMAYKGL FNIQFVLYDE ELYVIEVNPR
     ASRTVPIFSK ATSLPLITYT IDVLFGKTIA ELGLSAGYRK ESPYYTVKAP VFSYQKLAGL
     DPLLEAEMKS TGELIAISKD LPSAFRKAFA WGEEQTPALF RKKGSVFCQV DRAYDTEWQP
     LLRQLKEKGY SVVTEEAMSF SEWLASEDAI CLVSVPAPGQ KTGKQNREEA LKQRVTVVSD
     LATFEKMIEC LEVKDGEPFL LPDVVMN
//
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