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Database: UniProt
Entry: P14846
LinkDB: P14846
Original site: P14846 
ID   CARB_SALTY              Reviewed;        1075 AA.
AC   P14846; P96067;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   13-FEB-2019, entry version 146.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=carB; OrderedLocusNames=STM0067;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Lu C.D., Walthall D.A., Abdelal A.T.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC   STRAIN=LT2;
RX   PubMed=2843375; DOI=10.1111/j.1432-1033.1988.tb14299.x;
RA   Kilstrup M., Lu C.D., Abdelal A., Neuhard J.;
RT   "Nucleotide sequence of the carA gene and regulation of the carAB
RT   operon in Salmonella typhimurium.";
RL   Eur. J. Biochem. 176:421-429(1988).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
DR   EMBL; U81260; AAB39256.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19031.1; -; Genomic_DNA.
DR   EMBL; M36540; AAA27033.1; -; Genomic_DNA.
DR   RefSeq; NP_459072.1; NC_003197.2.
DR   RefSeq; WP_001126305.1; NC_003197.2.
DR   ProteinModelPortal; P14846; -.
DR   SMR; P14846; -.
DR   STRING; 99287.STM0067; -.
DR   PaxDb; P14846; -.
DR   PRIDE; P14846; -.
DR   EnsemblBacteria; AAL19031; AAL19031; STM0067.
DR   GeneID; 1251585; -.
DR   KEGG; stm:STM0067; -.
DR   PATRIC; fig|99287.12.peg.69; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   PhylomeDB; P14846; -.
DR   BioCyc; SENT99287:STM0067-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 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; 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   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; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
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; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2   1075       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145035.
FT   DOMAIN      133    328       ATP-grasp 1.
FT   DOMAIN      679    870       ATP-grasp 2.
FT   DOMAIN      937   1075       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000250}.
FT   NP_BIND     705    762       ATP. {ECO:0000250}.
FT   REGION        2    403       Carboxyphosphate synthetic domain.
FT   REGION      404    553       Oligomerization domain.
FT   REGION      554    936       Carbamoyl phosphate synthetic domain.
FT   REGION      937   1075       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       299    299       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       299    299       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       301    301       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       829    829       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       841    841       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       841    841       Magnesium or manganese 4. {ECO:0000250}.
FT   METAL       843    843       Magnesium or manganese 4. {ECO:0000250}.
FT   CONFLICT    123    123       I -> G (in Ref. 1; AAB39256).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1075 AA;  118139 MW;  918D74FADFF8CC7C CRC64;
     MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
     ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
     DAIDKAEDRR RFDIAMKKIG LDTARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGTGGG
     IAYNREEFEE ICERGLDLSP TNELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
     GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
     LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
     ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
     AYMYSTYEDE CEANPSIDRD KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
     CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
     VIGTSPDAID RAEDRERFQH AVDRLKLKQP ANATVTAIEQ AVEKAKEIGY PLVVRPSYVL
     GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDRFLDDAV EVDVDAICDG EMVLIGGIME
     HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKDNEVYLI
     EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLTEQGVT QEIIPPYYSV KEVVLPFNKF
     PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KQGRALLSVR EGDKERVVDL
     AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTAGR
     RAIEDSRVIR RSALQYKVHY DTTLNGGFAT TMALNADATE KVTSVQEMHA QIKKS
//
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