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
//