UniProt: F0NSN4

Database: UniProt
Entry: F0NSN4_LACHH

LinkDB:  F0NSN4_LACHH 
Original site:  F0NSN4_LACHH

All links

Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

Download RDF

ID   F0NSN4_LACHH            Unreviewed;      1063 AA.
AC   F0NSN4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:ADX70113.1};
GN   Name=carB {ECO:0000313|EMBL:ADX70113.1};
GN   OrderedLocusNames=LBHH_0903 {ECO:0000313|EMBL:ADX70113.1};
OS   Lactobacillus helveticus (strain H10).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=767462 {ECO:0000313|EMBL:ADX70113.1, ECO:0000313|Proteomes:UP000008640};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H10;
RA   Zhang H., Zhao W., Chen Y., Sun Z., Sun T., Meng H.;
RT   "Complete genome sequence of Lactobacillus helveticus strain H10.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADX70113.1, ECO:0000313|Proteomes:UP000008640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10 {ECO:0000313|EMBL:ADX70113.1,
RC   ECO:0000313|Proteomes:UP000008640};
RX   PubMed=21398542; DOI=10.1128/JB.00166-11;
RA   Zhao W., Chen Y., Sun Z., Wang J., Zhou Z., Sun T., Wang L., Chen W.,
RA   Zhang H.;
RT   "Complete genome sequence of Lactobacillus helveticus H10.";
RL   J. Bacteriol. 193:2666-2667(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   -!- 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}.
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; CP002429; ADX70113.1; -; Genomic_DNA.
DR   RefSeq; WP_014563503.1; NC_017467.1.
DR   AlphaFoldDB; F0NSN4; -.
DR   KEGG; lhl:LBHH_0903; -.
DR   PATRIC; fig|767462.3.peg.1006; -.
DR   HOGENOM; CLU_000513_1_2_9; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008640; 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   GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          132..335
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          676..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;  119368 MW;  09761050BE0EF166 CRC64;
     MPLENDLDKV LIIGSGPTLI GSVAEMDLMA TEAIDALTEE GIQVILVNPN PATISTDKKP
     NVTVYLEPMT LDFLKRILRM EEPDAIITAY GSTNGLKVAH KLLKDGILEQ MGIQLLTLNS
     RILQMGNQQK RTEFLNKLGI DTSESWELSQ TAQDNLIVAM DSLLAKVTFP VLVTKYNRYV
     HNEHLRFKNK EDLIVYFKEE SQTDNFTWKN YRLTEDLSAW EEVIVDVIRD KDENLVFTNF
     AGSIEPVAIN SGDSAVVMPS LTLNNDHIQE LRESVRRIVD NLGIVGFTSF HFAIKHHGTQ
     IKSKLLTIRP RLTRSSVWAQ RIGMYDVGYV VSKVAIGYRL NEITDPLSGL NASIEPTLDA
     IAIKIPYWSF TGSGYNHYQL SNRMQASGEA MGVGRNFETA FLKGLDATTN LDLGWNAFVE
     ESRKTNEEII ADLKHPDELH LIKLLAAIKE DIPFSELQQL TGLHPIYYQK LLHIVAIINK
     LVQNKEHLTL ELIKEAKDYG FFNPLLAKVL NISVEELRSL ISKYNLEPSF LKIDGSAGVY
     RPNVCAYYGA YDVQNEAKDL VADKKILILG MLPLQVSVTS EFDYMIAHAA KTLHKNGYVT
     VLLSNNDESV SSRYKDIDRV YFESITLENI LTIAKRENIK DVLLQFSGKR VSALSKQLEE
     NGLHIIGQSK TKDPRDTITD LLDHPLTNLK RVPSLKTTNP EAVFKFVDQY DFPILIGGMN
     KENKLKSAVV YDVPAIKRYL AENQVDQITV SQFIEGNKYE VTAISDGENV TLPGIIEHLE
     QTGSHASDSI AVIKPQNLSL EQQKKIEQQS IKLIKVLQTR GIFNLHYLRV NDELYLLQVK
     PYAGHNVAFL SKSLNKDITA CATEALIGHN LQELGYPNGL WHTSNFIHIK MPVFSFLNYS
     SGNTFDSNMK SSGSVMGRDT HLAKALYKGY EASDLHIPSY GTIFISVRDE DKNRVTELAR
     RFDRLGFKLI ATEGTANMFA EAGITTGVVE KVHNNPQNLL EKIRQHKIVM VVNITNLSDA
     ASEDALRIRD EALYTHIPVF SSIETAELIL DVLESLALTT QPI
//

DBGET integrated database retrieval system