CARB_STRP8
ID CARB_STRP8 Reviewed; 1058 AA.
AC P58941;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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}; OrderedLocusNames=spyM18_0895;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC 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 the
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL97546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009949; AAL97546.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011017652.1; NC_003485.1.
DR AlphaFoldDB; P58941; -.
DR SMR; P58941; -.
DR KEGG; spm:spyM18_0895; -.
DR HOGENOM; CLU_000513_1_3_9; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
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 CDD; cd01424; MGS_CPS_II; 1.
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 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; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1058
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145056"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 671..861
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 930..1058
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..546
FT /note="Oligomerization domain"
FT REGION 547..929
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 930..1058
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 697..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1058 AA; 116488 MW; D1BD1F05D01E0CAA CRC64;
MPKRKDIQKI MVIGSGPIII GQAAEFDYAG TQACLALKEE GYKVILVNSN PATIMTDKEI
ADKIYIEPLT LEFVNRIIRK ERPDAILPTL GGQTGLNMAM ALSKAGILDD LEIELLGTKL
SAIDQAEDRD LFKQLMQELD QPIPESTIVK TVDEAVTFAR DIGYPVIVRP AFTLGGTGGG
ICSSEEELCE ITENGLKLSP VTQCLIERSI AGFKEIEYEV MRDSADNALV VCNMENFDPV
GIHTGDSIVF APTQTLSDIE NQMLRDASLK IIRALKIEGG CNVQLALDPY SFKYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPITG TTYAMFEPAL DYVVAKIPRF
PFDKFEHGER QLGTQMKATG EVMAIGRNLE ESLLKACRSL EIGVCHNEMT SLSNISDEEL
VTKVIKAQDD RLFYLSEAIR RGYSIEELES LTKIDLFFLD KLLHIVEIEQ ELQMHVDHLE
SLKKAKRYGF SDQKIAEIWQ KDESDIRAMR HSHSLCPVYK MVDTCAAEFD AKTPYFYSTY
ELENESVQSN KESILVLGSG PIRIGQGVEF DYATVHSVKA IQKAGYEAII MNSNPETVST
DFSVSDKLYF EPLTFEDVMN VIDLEQPKGV IVQFGGQTAI NLAQSLSDAG VTILGTQVED
LDRAEDRDLF EKALKELGIP QPQGQTATNE EEALEAAKKI GFPVLVRPSY VLGGRAMEIV
ENKEDLREYI RTAVKASPEH PILVDSYIFG KECEVDAISD GKSVLIPGIM EHIERAGVHS
GDSMAVYPPQ QLSKQIQETI AEYTKRLAIG LNCIGMMNVQ FVIKNEQVYV IEVNPRASRT
VPFLSKVTGI PMAQIATKLI LGQTLKDLGY EDGLYPQSQL VHIKAPVFSF TKLAQVDSLL
GPEMKSTGEV MGSDTSLEKA LYKAFEANNS HLSEFGQIVF TIADDSKAEA LSLARRFKAI
GYQIMATQGT AAYFAEQGLS ACLVGKIGDA ANDIPTLVRH GHVQAIVNTV GIKRTADKDG
QMIRSSAIEQ GVPLFTALDT AKAMLTVLES RCFNIEAI
