ID C0EZ47_9FIRM Unreviewed; 1077 AA.
AC C0EZ47;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 86.
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 ECO:0000313|EMBL:EEG35482.1};
GN ORFNames=EUBHAL_02703 {ECO:0000313|EMBL:EEG35482.1};
OS Anaerobutyricum hallii DSM 3353.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerobutyricum.
OX NCBI_TaxID=411469 {ECO:0000313|EMBL:EEG35482.1, ECO:0000313|Proteomes:UP000003174};
RN [1] {ECO:0000313|EMBL:EEG35482.1, ECO:0000313|Proteomes:UP000003174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG35482.1,
RC ECO:0000313|Proteomes:UP000003174};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG35482.1, ECO:0000313|Proteomes:UP000003174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG35482.1,
RC ECO:0000313|Proteomes:UP000003174};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium hallii (DSM 3353).";
RL Submitted (FEB-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEG35482.1}.
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DR EMBL; ACEP01000119; EEG35482.1; -; Genomic_DNA.
DR RefSeq; WP_005350103.1; NZ_ACEP01000119.1.
DR AlphaFoldDB; C0EZ47; -.
DR GeneID; 75049052; -.
DR eggNOG; COG0458; Bacteria.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000003174; Unassembled WGS sequence.
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; 3.30.470.20; 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_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 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}; Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 673..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 932..1077
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT REGION 932..1077
FT /note="Allosteric domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1077 AA; 119120 MW; 7288EACFF93B775E CRC64;
MPKNTSIKKV LVIGSGPIVI GQAAEFDYAG TQACRSLKEE GIHVVLVNSN PATIMTDKDI
ADEVYIEPLT PEVIKKLILK VSPDSLLPTL GGQAALNIAM ELDECGFLKE HKVKLIGTTG
KTIRKAEDRE EFKETMEKIG EPIAPSQIVT NVEDGLEYAQ KIGYPVVLRP AYTLGGSGGG
IADNEEEFVE IIQNGLRLSR VGQVLVEKSI AGWKEIEYEV MRDGNGTCIT VCNMENLDPV
GVHTGDSIVV APSQTLGDKE YQMLRNSALN IIDELGVEGG CNVQFALNPD TFDYCVIEVN
PRVSRSSALA SKATGYPIAK VTAKIALGYH LDEIKNAVTG KTFASFEPAL DYCVVKVPRL
PFDKFISASR HLTTQMKATG EVMSICTNFE GGLMKALRSL EQHVDSLMHG DFDKLSDKEL
EEHLHIVDDL RIYCIAEALR RKVNPQKIHD ITKIDLWFID KLNNIVEMEA KLKNAEELDR
DLLLKAKEME FPDKVIGELI GQSEEYVKNL RRQMDIVPAY KVVDTCAAEF AAETPYYYSC
FGSFNEVEET SDKKKIMVLG SGPIRIGQGI EFDYCSVHSV WAFKEMGYET IIVNNNPETV
STDFDIADKL YFEPLTEEDV EHIVELEKPD GAVVQFGGQT AIKLTEKLNK IGVPILGTSA
ENVDAAEDRE LFDEILEQCC IPRPKGGTVF TKEEAIKTAN EIGYPVLIRP SYVLGGQGMQ
IAISDEDISE FMDVIQRYAQ EHPILIDKYL MGVEVEVDAV CDGEEIVIPG IMQHVERAGI
HSGDSISVYP ARDLSPKIKK VIGHYTKLLA KALHVIGLIN IQFIVYQDEV YVIEVNPRSS
RTVPYISKVT GIPIVDLATK VMTGMKLKDL GYEPGLQPES PYWAIKMPVF SFEKIRGADI
SLGPEMKSTG ECLGISKNFE EALFKAFLGS GVDLPKHKKM IMTVKDSDKL DAVEVGKRFT
ALGYEIYATR NTCKTLQESG VPAKRVNKIE ESHPNLLDLI LGHQIDLIID TPSQGIERSK
DGFVIRRHAV ETGVNCLTSL DTANALLTSL ESSCREDLSL VDIAEIDKEI ESKINEA
//