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Database: UniProt
Entry: A2BJL3
LinkDB: A2BJL3
Original site: A2BJL3 
ID   CARB_HYPBU              Reviewed;        1073 AA.
AC   A2BJL3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   16-JAN-2019, entry version 79.
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};
GN   OrderedLocusNames=Hbut_0302;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Pyrodictiaceae; Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
RA   Awayez M., She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-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
CC       the 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}.
DR   EMBL; CP000493; ABM80174.1; -; Genomic_DNA.
DR   RefSeq; WP_011821492.1; NC_008818.1.
DR   ProteinModelPortal; A2BJL3; -.
DR   SMR; A2BJL3; -.
DR   STRING; 415426.Hbut_0302; -.
DR   PRIDE; A2BJL3; -.
DR   EnsemblBacteria; ABM80174; ABM80174; Hbut_0302.
DR   GeneID; 4781404; -.
DR   KEGG; hbu:Hbut_0302; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 911at2157; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002593; 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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 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; IPR036914; MGS-like_dom_sf.
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; 1.
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; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1073       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066351.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      681    871       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      944   1073       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     707    764       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    555       Oligomerization domain.
FT   REGION      556    944       Carbamoyl phosphate synthetic domain.
FT   REGION      945   1073       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       830    830       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       844    844       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1073 AA;  119163 MW;  7EBC60AE6A97BACC CRC64;
     MPRRIDVRKV LMLGSGAIKI AEAAEFDYSG SQALKALREE GIETVLVNPN VATIQTSYKL
     ADHVYLGPLQ PWFVEKVIER ERPDAILLGF GGQTALSLGV ELHRRGILSR YGIRVLGTPI
     EGIEKALSRG KFRETMMKAG LPVPPSTPAT SVEEALRAAN EIGYPVIVRV SFNLGGGGSL
     VAWSREELER WLVRAFAFSG TGEVLVEKYL HYWKEIEYEV VRDQYGNMVA VACLENADPM
     GVHTGESVVI APCQTLTDQE YQLLREASLR VAEAIGLVGE GNVQLALNPR DSWEYYVIET
     NPRMSRSSAL ASKATGYPLA YIAAKLALGY RLDELLNRVT ERTCACFEPS LDYVVVKVPR
     WDLEKFEGVE KSIGSEMKSI GEVMAIGRNF AEALQKAIRM LDIGEPGVVA GPRYEEPESL
     EEVLGKLRRR EPYWPIWAAK AFRLGASVEQ VYEATGVDPY FLSQIREIVE VAEKLRRTKP
     WSSEFLDLLA EAKRLGFSDE QVALLTGTTV EKVEKARRSI GLDRPRVRQI DTLAAEWPAA
     TNYLYMSYNA YEDDEPITTG RPRLIVLGAG VFRIGVSVEF DWGVVSFADE ARRLGYEVVI
     VNYNPETVST DWDISDKLYF EELTLERVID IYWFEKPVGV IAFLGGQIAN NLAKPLEERG
     VRLLGTPGRS VDRAENRAWF SQLLEELGIK QPSWTAASSI EEVLKFAESV GYPVLVRPSY
     VLSGSAMKIA WSPEELKSYI EQAARVSPRY PVVVSKFLED AVEAEIDAVG DSRRTVGTVI
     EHVEPGGVHS GDSTMVIPWF SLPETAVREM IRIAETLNEV LEIKGPFNIQ FLVKDGSVYV
     VELNLRASRS MPFTSKVTGY NLMRAAAEAA LRGRISYGFN GADGFKLLRP TGWWGVKSPQ
     PSWQRLRGAY PGLGPEMRST GEVAALGRTL HEALLKSWLS VQGNRIPPAG SIVLIYTPTG
     RGSSDLSQAA KLMTEKGYTV YTIEGMEVDG AEPLPLEQAL RLVRMGGVGL LMTTDYAPQR
     DYRVRRLAVD LGVPVVLDAR LARMLAEAIN RVGLENLEAL ELREYWGPNV EPF
//
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