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 01-MAY-2013, entry version 35.
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.
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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; GMINIQF; -.
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:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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_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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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
//
