CARB_BRUME
ID CARB_BRUME Reviewed; 1162 AA.
AC Q8YIC2;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=BMEI0522;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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}.
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DR EMBL; AE008917; AAL51703.1; -; Genomic_DNA.
DR PIR; AD3317; AD3317.
DR RefSeq; WP_004684046.1; NZ_GG703780.1.
DR AlphaFoldDB; Q8YIC2; -.
DR SMR; Q8YIC2; -.
DR STRING; 224914.BMEI0522; -.
DR PRIDE; Q8YIC2; -.
DR EnsemblBacteria; AAL51703; AAL51703; BMEI0522.
DR GeneID; 29593304; -.
DR KEGG; bme:BMEI0522; -.
DR PATRIC; fig|224914.52.peg.947; -.
DR eggNOG; COG0458; Bacteria.
DR OMA; IEPAGIH; -.
DR PhylomeDB; Q8YIC2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000419; Chromosome I.
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; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
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; 1.
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..1162
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000144993"
FT DOMAIN 186..381
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 742..954
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 1026..1162
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..456
FT /note="Carboxyphosphate synthetic domain"
FT REGION 457..613
FT /note="Oligomerization domain"
FT REGION 614..1025
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 1026..1162
FT /note="Allosteric domain"
FT BINDING 212..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 768..846
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 913
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 925
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 925
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 927
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1162 AA; 126360 MW; E8320AD5A7AAD85E CRC64;
MPKRTDIKSI LIIGAGPIVI GQACEFDYSG TQACKALKEE GYRIILVNSN PATIMTDPDL
ADATYIEPIT PEVVAKIIAK ERPDAILPTM GGQTALNTAL SLRRMGVLER YNVEMIGAKA
EAIDKAEDRA LFREAMKKIG LDTPGSMFAN ATEIKDEDRK RHEVKRAEVK AQFSGDELDK
ALDKLETEWQ LGEVERKQRY MSHALAKAAQ ALDVVGLPAI IRPSFTLGGT GGGIAYNRQE
FFEIIERGLD ASPTTEVLIE ESVLGWKEYE MEVVRDHADN CIIICSIENL DPMGVHTGDS
ITVAPALTLT DKEYQIMRNA SIAVLREIGV ETGGSNVQFA INPANGRMIV IEMNPRVSRS
SALASKATGF PIAKVAAKLA VGYTLDELDN DITGGATPAS FEPSIDYVVT KIPRFAFEKF
PGSSPILTTA MKSVGEVMAI GRTFQESLQK ALRGLETGLT GFDEIAIPNI EEGDEKNAIR
AAIGTPTPDR LRMVAQAMRL GLSVEQVHDA SKIDPWFLEQ IESIVKTEER IREHGLPQDA
ENLRMLKAMG FSDARLASLT AKDAEDVAKL RADLDVHPVY KRIDTCAAEF ASPTAYMYST
YETPFVGQPR SEAEVSDRKK VVILGGGPNR IGQGIEFDYC CCHAAFALGD ADYEAIMVNC
NPETVSTDYD TSDRLYFEPL TAEDVLEILR VEKQKGTLHG VIVQFGGQTP LKLANALEKA
GIPILGTSPD AIDLAEDRDR FQKLLIKLDL NQPKNGIAYS VEQARLVAAD LGFPLVVRPS
YVLGGRAMQI IHDERGLQAY LLDTVPELVP EDIKAKYPND KTGQINTLLG KNPLLFDTYL
TEAIEVDVDC LCDGKDSLVA GIMEHIEEAG IHSGDSACLL PVHTLSPEIV AELERQTAAL
ATALHVGGLM NVQFAIKDGE IFILEVNPRA SRTVPFVAKT VGTPIAKVAA RIMAGESLEA
AFDAYGGKPQ PTARPHIAVK EAVFPFARFP GVDTLLGPEM RSTGEVMGLD YDYALAFAKA
QLGAGVELPR EGTVFVSVRD EDKERVLGPV RKLASIGFKV MATGGTQKFL EANGVESTKI
NKVIEGRPHV EDAIRNRQIH LVFNTTDSAS AVSDSKSIRR ATLMQKLPYY TTMAGAESAA
EAIAALKAGS LEVRPLQDYF RS
