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Database: UniProt
Entry: A9WSA8
LinkDB: A9WSA8
Original site: A9WSA8 
ID   CARB_RENSM              Reviewed;        1106 AA.
AC   A9WSA8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JAN-2019, entry version 75.
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=RSal33209_1963;
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484
OS   / NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S.,
RA   Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J.,
RA   Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum
RT   suggests reductive evolution away from an environmental Arthrobacter
RT   ancestor.";
RL   J. Bacteriol. 190:6970-6982(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; CP000910; ABY23696.1; -; Genomic_DNA.
DR   RefSeq; WP_012245366.1; NC_010168.1.
DR   ProteinModelPortal; A9WSA8; -.
DR   SMR; A9WSA8; -.
DR   STRING; 288705.RSal33209_1963; -.
DR   EnsemblBacteria; ABY23696; ABY23696; RSal33209_1963.
DR   KEGG; rsa:RSal33209_1963; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; RSAL288705:G1GAP-1745-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002007; 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   1106       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000085561.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      677    868       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      957   1106       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     703    760       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    548       Oligomerization domain.
FT   REGION      549    956       Carbamoyl phosphate synthetic domain.
FT   REGION      957   1106       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       827    827       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       839    839       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       839    839       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1106 AA;  118225 MW;  8AD1A81DBA7A795E CRC64;
     MPKREDLKSV LVIGSGPIVI GQAAEFDYSG TQALRVLKEE GLRVILVNSN PATIMTDPEF
     ADATYVEPIT PEVVEKIIAK ERPDALLPTL GGQTALNTAI ALDKNGVLAK YNVELIGANI
     AAIELGEDRE KFKGVVERCG AESARSHIVH AMDEALVAAA DLGYPLVVRP SFTMGGLGSG
     LAYNEKDLHR IAGAGLQYSP TSEVLLEESI LGWKEYELEM MRDKNDNVVV VCSIENFDPV
     GVHTGDSITV APAMTLTDRE YQNLRDISIA VIREVGVDTG GCNIQFAIEP DTGRVVVIEM
     NPRVSRSSAL ASKATGFAIA KIATKLSLGY TLDEIPNDIT QKTPASFEPT LDYVVVKVPR
     FAFEKFPAAD PTLTTTMKSV GEAMAIGRNF TEALQKALRS LEQKGSQLDF GSVNALDVPE
     LIEAAKRPTT DRLGQVQRAL AGGASVEDLY AATGIDPWFL EQLQLLNEVA VELKQAPQLH
     ESLLRKAKRH GFSDEQIAGL TNNAEAVVRG VRQALGIRPV YKTVDTCAAE FAAYTPYHYS
     SYDQEDEIAL HEKPSVIILG SGPNRIGQGI EFDYSCVHAS MALRKAGYET VMVNCNPETV
     STDYDVSTRL YFEPLTLEDV LEVIAAEERT GGVMGVFVQL GGQTPLKLAQ DLADAGVPIL
     GTPPEAIDLA EHRGQFARVL DIAGLIAPKN GAAVSFEDAK RVADEIGYPV LVRPSYVLGG
     RGMEIVYDEP NLLRYITNAT EITPDHPVLI DRFLEDAIEI DVDALYDGKE LYLGGVMEHI
     EEAGIHSGDS ACVLPPITLG QGVVDRVRDA TQAIAEGVGV RGLINIQFAL ASDVLYVLEA
     NPRASRTVPF VSKATGVQLA KAAALIGTGV TINQLRTAYK MIPSLPGTPG GFDGGSLPVG
     APVAVKEAVL PFSRFRTPEG AVVDSLLGPE MRSTGEVMGI DKHFDTAFAK SQAAANNALP
     TEGKVFVSVA NRDKRAVIMA VKLLADLGFE IVSTGGTADV LRRNGIQSST VRKVAEGTSA
     EGEGTITDLI IAGEIDMVFN TPSGGEARGD GYEIRAAAIS IGIPCITTVA EFNVAVLAIE
     AMRSFEWNVT SLQEHAEALL EAAANV
//
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