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Database: UniProt
Entry: Q8YIC2
LinkDB: Q8YIC2
Original site: Q8YIC2 
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   05-DEC-2018, entry version 115.
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=BMEI0522;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; 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
RT   Brucella 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;
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; AE008917; AAL51703.1; -; Genomic_DNA.
DR   PIR; AD3317; AD3317.
DR   RefSeq; WP_004684046.1; NZ_GG703780.1.
DR   ProteinModelPortal; Q8YIC2; -.
DR   SMR; Q8YIC2; -.
DR   STRING; 224914.BAWG_2501; -.
DR   PRIDE; Q8YIC2; -.
DR   EnsemblBacteria; AAL51703; AAL51703; BMEI0522.
DR   GeneID; 29593304; -.
DR   KEGG; bme:BMEI0522; -.
DR   KEGG; bmel:DK63_902; -.
DR   PATRIC; fig|224914.52.peg.947; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; BMEL224914:G1FZL-563-MONOMER; -.
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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1162       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000144993.
FT   DOMAIN      186    381       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      742    954       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN     1026   1162       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     212    269       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     768    846       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    456       Carboxyphosphate synthetic domain.
FT   REGION      457    613       Oligomerization domain.
FT   REGION      614   1025       Carbamoyl phosphate synthetic domain.
FT   REGION     1026   1162       Allosteric domain.
FT   METAL       338    338       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       352    352       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       352    352       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       354    354       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       913    913       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       925    925       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       925    925       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       927    927       Magnesium or manganese 4.
FT                                {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
//
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