ID G5QD42_SALRU Unreviewed; 353 AA.
AC G5QD42;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:EHC96237.1};
DE Flags: Fragment;
GN ORFNames=LTSERUB_0102 {ECO:0000313|EMBL:EHC96237.1};
OS Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC96237.1, ECO:0000313|Proteomes:UP000004903};
RN [1] {ECO:0000313|EMBL:EHC96237.1, ECO:0000313|Proteomes:UP000004903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-653 {ECO:0000313|EMBL:EHC96237.1,
RC ECO:0000313|Proteomes:UP000004903};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:EHC96237.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFCT01000065; EHC96237.1; -; Genomic_DNA.
DR AlphaFoldDB; G5QD42; -.
DR PATRIC; fig|913081.3.peg.160; -.
DR Proteomes; UP000004903; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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 PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 12..203
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 270..353
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC96237.1"
SQ SEQUENCE 353 AA; 38784 MW; 60E672266A07A14C CRC64;
AIDRAEDRER FQHAVDRLKL KQPANATVTA IEQAVEKAKE IGYPLVVRPS YVLGGRAMEI
VYDEADLRRY FQTAVSVSND APVLLDRFLD DAVEVDVDAI CDGEMVLIGG IMEHIEQAGV
HSGDSACSLP AYTLSQEIQD VMRQQVQKLA FELQVRGLMN VQFAVKDNEV YLIEVNPRAA
RTVPFVSKAT GVPLAKVAAR VMAGKSLTEQ GVTQEIIPPY YSVKEVVLPF NKFPGVDPLL
GPEMRSTGEV MGVGRTFAEA FAKAQLGSNS TMKKQGRALL SVREGDKERV VDLAAKLLKQ
GFELDATHGT AIVLGEAGIN PRLVNKVHEG RPHIQDRIKN GEYTYIINTS CFM
//
