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CARB_RENSM
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   03-AUG-2022, entry version 86.
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; 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., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter 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; 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; CP000910; ABY23696.1; -; Genomic_DNA.
DR   RefSeq; WP_012245366.1; NC_010168.1.
DR   AlphaFoldDB; A9WSA8; -.
DR   SMR; A9WSA8; -.
DR   STRING; 288705.RSal33209_1963; -.
DR   EnsemblBacteria; ABY23696; ABY23696; RSal33209_1963.
DR   KEGG; rsa:RSal33209_1963; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_11; -.
DR   OMA; IEPAGIH; -.
DR   OrthoDB; 48855at2; -.
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; 3.30.1490.20; -; 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; 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; Reference proteome; Repeat.
FT   CHAIN           1..1106
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_1000085561"
FT   DOMAIN          133..328
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          677..868
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          957..1106
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   REGION          1..402
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          403..548
FT                   /note="Oligomerization domain"
FT   REGION          549..956
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          957..1106
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         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         703..760
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         827
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         839
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         839
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         841
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="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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