ID Q1GA90_LACDA Unreviewed; 1063 AA.
AC Q1GA90;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Carbamoyl-phosphate synthase, large chain {ECO:0000313|EMBL:CAI97826.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:CAI97826.1};
GN Name=carB3 {ECO:0000313|EMBL:CAI97826.1};
GN Synonyms=pyrAB3 {ECO:0000313|EMBL:CAI97826.1};
GN OrderedLocusNames=Ldb1024 {ECO:0000313|EMBL:CAI97826.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97826.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI97826.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CR954253; CAI97826.1; -; Genomic_DNA.
DR RefSeq; WP_003622888.1; NZ_JQAV01000013.1.
DR AlphaFoldDB; Q1GA90; -.
DR STRING; 390333.Ldb1024; -.
DR KEGG; ldb:Ldb1024; -.
DR PATRIC; fig|390333.13.peg.665; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_2_9; -.
DR BioCyc; LDEL390333:LDB_RS04490-MONOMER; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001259; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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 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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 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; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAI97826.1};
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|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000001259};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 681..867
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 935..1063
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1063 AA; 118917 MW; F8A9DD489070ED2A CRC64;
MPRENDLNKI LIIGAGSALV GNVANTDLLT KSAIEALLEE NIQVVLVNPN PASVSTDPLP
GLTVYLEPMT LDFLKRILRM EEPDAIMTAF GSLMALDVTK KLQADGILHQ MGIKLLTINE
RAISMSNPQK RTRFLEANHL PVGQTWFLDS LGLKYDEHLQ EQLENKLSFP ILLTKKYYFE
RDDHISFKSS RDLAQYLRQE SQDRDFRPAS YRMTEDLSNC EEVILDLLRD EDGNLCFVGA
TGSLEPVGID SGDSVLIKPL LTMNNDQIQV LRAEAGKIAD KLQLVGFLSV HFAISHRGTE
MVYKLLAVKP RLTRTAVMDQ KTSLYSIGYV LAKLAIGLRL NEVTDPATGL CAAIEPVSDT
VSIKIPYWSF AKTGYNHYQL GKHTQSTGEA VGIGRNFESA FFKALISSND LEVLWSAFIK
ERGKSDEVIL DDLRHPNEMH LVQLLAALSQ GIDYQAISSV LNIHPVYYQK LRYLVKIGRD
IAHAGELDHD LLLKAKIRGF SSDLLAELTK MDVHDIFPLL NEKDVRPTFS AIDDSAGVYQ
PKVKVYYQSY GVESELEFAK DPEKKKVLLL GMPPFQVSVT SEFDYMLYHA LAALKKEGYE
TVLLSNNAES ASMDYHLADR VYFEPINLDS IITICEEEGI TDVVTQFSGK QISALRLPLM
SHGLKIFGQH EIDRLLPISH LDTAKISEVK RVPYLATTDY QAVLAFVARV GYPVLVGGYH
QKSKQKSAVI YDQPALEKYF RENQVDNYTI SQFISGVKYE ITAITDGEDV TIPGIVEHLE
QSGSHASDSI AVFGPQYLSK EQAEKLRVET IKLIRSFKIR GIFNLHFLLK GREIYLLQIK
TYAGHNLAFL SKSMNKDLVE YAVKVLAGRK IADLGYPNEV WPVDEFIHVK MPVFSYLNYS
SDNTFDSRMK SSDAVMGRDS RLAKALYKGY EASDLHIPSY GTIFFSVSDE EKQEVANLAK
RFARLGFKIT ATEGTANILA EAGITTGVIA KIQEGSRNLL ERIQTHRIVM VVNVVNLSDS
AVEDSIKIKD QALNTHIPVF SSLETVQLIL DVLESLALTT QPI
//
