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Database: UniProt
Entry: B0REV9
LinkDB: B0REV9
Original site: B0REV9 
ID   CARB_CLAMS              Reviewed;        1096 AA.
AC   B0REV9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 81.
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=CMS2029;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM
OS   20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis
RT   subsp. sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ02125.1; -; Genomic_DNA.
DR   RefSeq; WP_012299351.1; NZ_MZMN01000003.1.
DR   ProteinModelPortal; B0REV9; -.
DR   SMR; B0REV9; -.
DR   STRING; 31964.CMS_2029; -.
DR   EnsemblBacteria; CAQ02125; CAQ02125; CMS2029.
DR   GeneID; 29470581; -.
DR   KEGG; cms:CMS2029; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001318; Chromosome.
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; 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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1096       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000085555.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      676    870       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      951   1095       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     702    762       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    547       Oligomerization domain.
FT   REGION      548    950       Carbamoyl phosphate synthetic domain.
FT   REGION      951   1096       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       829    829       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       843    843       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1096 AA;  117554 MW;  9602A1069C076C8B CRC64;
     MPKRDDINSV LVIGSGPIVI GQAAEFDYSG TQACRVLREE GVRVILVNSN PATIMTDPGF
     ADATYIEPIT SEVLEKIIIK ERPDAVLPTL GGQTALNAAI RLDELGILAK HGVELIGAKV
     EAIQKGEDRQ LFKDLVIESG ADVARSHVAK TLEQAVEFAE DLGYPLVIRP SFTMGGLGSG
     FAHTRQELER MVADGLQSSP TTEVLLEESI LGWKEYELEL MRDTADNTVV VCSIENVDPV
     GVHTGDSITV APALTLTDRE YQHMRDIGID IIRRVGVDTG GCNIQFAVDP TNGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAIGY RLDEIPNDIT KVTPASFEPT LDYVVVKVPR
     FAFEKFPAAD AELTTTMKSV GEAMAIGRNY STALQKALRS LEKRGSSFHW GAESRSVEEL
     LETSRIPTDG RIVTVQQALR AGATPEQVFD ATKIDPWFID QIVLINEVAD AVRDADELDA
     PTLREAKDHG FSDAQIAEIR GIGEQEVRDA RHAAGIRPVF KTVDTCAGEF PALTPYHYSS
     YDSETEIVPS DRRKVIILGS GPNRIGQGIE FDYSCVHASF ALADAGFETI MINCNPETVS
     TDYDTSDRLY FEPLTLEDVL EIVHVEQQAG ELVGVVVQLG GQTALGLAKG LEAAGVPILG
     TSPSAIDLAE ERGLFSGILD AAGLVAPRNG TAVAIDEAVV VAEEIGYPVL VRPSYVLGGR
     GMEIVFDTAT LHDYFLRMAD QGIIGEGKPL LIDRFLDDAI EIDIDAIYDG TELYVGGVME
     HIEEAGIHSG DSSCTLPPVT LGRGQIQQVV DATRAIAEGV GVRGLLNVQF AIGAGVLYVL
     EANPRASRTV PFVSKALGIP LAKAASLVMV GTSIAELKAS GLLPERDGSD VPMDSPVAVK
     EAVLPFKRFR TKDGLIVDSV LGPEMRSTGE VMGIDRDFPR AFAKSQEAAF GGLPLSGTVF
     VSVADRDKRS IVLPVLRLQQ LGFEVLATAG TAEILSRNGI QARVVRKYSE EPAAGDSPSI
     VDLINRDEVD VVINTPSGRT ARADGYEIRA AAVAADKPLF TTIAQLTAAV ASFDAIRAGF
     DVTSLQDYAI AREARR
//
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