GenomeNet

Database: UniProt
Entry: C0M756
LinkDB: C0M756
Original site: C0M756 
ID   CARB_STRE4              Reviewed;        1058 AA.
AC   C0M756;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   19-FEB-2014, entry version 38.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=carB; OrderedLocusNames=SEQ_1313;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K.,
RA   Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K.,
RA   Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K.,
RA   Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M.,
RA   Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J.,
RA   Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CarB family.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FM204883; CAW94096.1; -; Genomic_DNA.
DR   RefSeq; YP_002746594.1; NC_012471.1.
DR   ProteinModelPortal; C0M756; -.
DR   STRING; 553482.SEQ_1313; -.
DR   EnsemblBacteria; CAW94096; CAW94096; SEQ_1313.
DR   GeneID; 7696582; -.
DR   KEGG; seu:SEQ_1313; -.
DR   PATRIC; 19647418; VBIStrEqu13040_1328.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; FDKFQGA; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; SEQU553482:GJOY-1300-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 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; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 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.
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; Repeat.
FT   CHAIN         1   1058       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164715.
FT   DOMAIN      133    327       ATP-grasp 1.
FT   DOMAIN      671    861       ATP-grasp 2.
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     697    754       ATP (By similarity).
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    546       Oligomerization domain.
FT   REGION      547    929       Carbamoyl phosphate synthetic domain.
FT   REGION      930   1058       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 2 (By similarity).
FT   METAL       300    300       Magnesium or manganese 2 (By similarity).
FT   METAL       820    820       Magnesium or manganese 3 (By similarity).
FT   METAL       832    832       Magnesium or manganese 3 (By similarity).
FT   METAL       832    832       Magnesium or manganese 4 (By similarity).
FT   METAL       834    834       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1058 AA;  116214 MW;  348B0DB103133F8A CRC64;
     MAKRTDIKKI MVIGSGPIVI GQAAEFDYAG TQACLALKEE GYQVVLVNSN PATIMTDKEV
     ADKVYIEPLT LAFVSRILRK ERPDALLPTL GGQTGLNMAM ELSKAGILQE LGVELLGTTL
     SAIDQAEDRD LFKQLMKELG EPIPESEIVT TVEAAIGFAN AIGYPVIVRP AFTLGGTGGG
     ICSNEEVLRD IVENGLKLSP VTQCLIERSI AGFKEIEYEV MRDAADNALV VCSMENFDPV
     GIHTGDSIVF APTQTLSDVE NQLLRDASLR IIRALKIEGG CNVQLALDPN SFSYYVIEVN
     PRVSRSSALA SKATGYPIAK IAAKIAVGLR LDDMLNPVTG TTYAMFEPAL DYVVAKLPRF
     PFDKFERGER RLGTQMKATG EVMAIGRRIE ECLLKACRSL EIGVHHNELK GLDTISDHEL
     VAHIVRAQDD RLFYLSEALR RGYSIEELAG LTKIDLFFLD KLRHIVELEQ DLIKKPVDID
     LLIEAKRYGF SDQKIAELWQ TDAASIRRLR RAYRVLPVYK MVDTCAAEFD SQTPYFYSTY
     EWENESIKSE KESVIVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
     DFSISDKLYF EPLTFEEVMN VIELEQPKGV ILQFGGQTAI NLAEQLTKAG VPILGTQLED
     LDCAEDRELF EKALKELGIP QPPGKTATNE AEALEAARAI GFPVLVRPSY VLGGRAMEIV
     ENENDLRSYM KTAVKASPEH PVLIDSYILG KECEVDAISD GQSVLIPGIM EHIERAGVHS
     GDSMAVYPPQ HLSKQVQDKI VDYTKRLAIG LNCIGMMNIQ FVIQNEQVYV IEVNPRASRT
     VPFLSKVTNI PMAQVATKLI LGQTLKDLGY QDGLYPESSL VHIKAPVFSF AKLAKVDSLL
     GPEMKSTGEV MGSDLTLEKA LYKAFEASYL HMPEYGTIVF TIADDHKSEA LILARRFSAI
     GYQIMATEGT AAFFADQGLD SQLVGKIGDN AHDIPALLRK GQIQAIINTV GTKRVTDKDG
     QMIRSSAIEQ GVPLFTALDT AVAMLRVLES RTFSIEAI
//
DBGET integrated database retrieval system