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Database: UniProt
Entry: L0F8N0_DESDL
LinkDB: L0F8N0_DESDL
Original site: L0F8N0_DESDL 
ID   L0F8N0_DESDL            Unreviewed;      1058 AA.
AC   L0F8N0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=Desdi_2767 {ECO:0000313|EMBL:AGA70179.1};
OS   Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA70179.1, ECO:0000313|Proteomes:UP000010797};
RN   [1] {ECO:0000313|Proteomes:UP000010797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA   de Vos W.M., Boon N., Smidt H., Woyke T.;
RT   "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP-
CC         Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01210};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01210};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812, ECO:0000256|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 the
CC       large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|ARBA:ARBA00009799,
CC       ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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DR   EMBL; CP003344; AGA70179.1; -; Genomic_DNA.
DR   RefSeq; WP_015263145.1; NC_019903.1.
DR   AlphaFoldDB; L0F8N0; -.
DR   STRING; 871963.Desdi_2767; -.
DR   KEGG; ddl:Desdi_2767; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_3_9; -.
DR   OMA; QFIEFEG; -.
DR   OrthoDB; 9804197at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000010797; 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; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 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   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
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; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
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 {ECO:0000256|HAMAP-Rule:MF_01210};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01210};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01210};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01210};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01210}; Reference proteome {ECO:0000313|Proteomes:UP000010797};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}.
FT   DOMAIN          132..326
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          670..860
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          929..1058
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..400
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          546..928
FT                   /note="Carbamoyl phosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          929..1058
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         819
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         831
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         831
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         833
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1058 AA;  116369 MW;  4E15C254BB560441 CRC64;
     MKNKKWNKVL VIGSGPIVIG QAAEFDYAGT QACRALREEG VEVVLVNSNP ATIMTDQEVA
     DRVYIEPLTV EFLERIIERE RPDGLIPTMG GQTGLNLAFQ LAERGILDRC GVQLMGTSLE
     SITKAEDREH FRSLMNSLGE PVPPSVIVSE VEEALDFAEE IGFPVIVRPA YTLGGTGGGI
     AQDRQSLQEI CKSGLQASLI GQILVEKSVA GWKEIEYEVL RDGAGNCITI CNMENMDPVG
     VHTGDSIVVA PCQTLTDREV QALRTSSRRI VEALGIEGGC NVQYALHPER LDYVVIEVNP
     RLSRSSALAS KATGYPIAKV AAKIALGYTL PELTNAVTGK TSACFEPALD YVVVKIPRWP
     FDKFSDADRR LGTQMKATGE VMGLGRNLET ALQKAVRSLE IKAYGLLLPE LEGLSDEEIL
     NRCQKPDDQL LFILAEGFRR GFSLERIQKA SHWNPYFLLA IQRIVKLSYE LQTSPWHQEL
     LLKAKRMGFA DREIARLWKT TEKELYDYRE DKGIHPVFKM VDTCAGEFEA LTPYFYSSYD
     QENEGIPSPK RKVVVLGSGP IRIGQGIEFD YCSVHSVLAL KKAGVETIII NNNPETVSTD
     FDTADRLYFE PLTLEDVSAV LDLEQPEGVI VQFGGQTAIG LAKPLAERGY KILGTSIEDI
     DRAEERGLFD EVLNAIGAKR PKGGQASSLK EARDVAAQIG YPLMIRPSFV LGGRAMEIVY
     DPTELENVVN RAMADFPGQE LWMDQYLVGT EVEVDAISDG ENVSIPGIME HLERAGVHSG
     DSIAVYPPLT LPEPLKERIT LLTTEIARTL NVLGLLNIQY VIYQGEVYVI EVNPRSSRTV
     PFISKVTGLS IVDYATDVIM GKTLPELNLP LGLWPVPDRV AVKVPVFSFS KLHRVEPSLG
     PEMKSTGEVM GVDRTYEKAL YKALLAGGFN MSAHGSLLVT LADRDKQEGL SLVKKFVDLG
     FRILATEGTA KALREEEIEV IPVAKLHQGS TEITDAIRQG VIQCVLNTTT HNKKQASDGF
     AIRRTAVEQG IPCFTSLDTA SAWVHVLMSF LPSLMPLS
//
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