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Database: UniProt
Entry: P25994
LinkDB: P25994
Original site: P25994 
ID   CARB_BACSU              Reviewed;        1071 AA.
AC   P25994;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   13-FEB-2019, entry version 144.
DE   RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=pyrAB; OrderedLocusNames=BSU15520;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1709162;
RA   Quinn C.L., Stephenson B.T., Switzer R.L.;
RT   "Functional organization and nucleotide sequence of the Bacillus
RT   subtilis pyrimidine biosynthetic operon.";
RL   J. Biol. Chem. 266:9113-9127(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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: 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; M59757; AAA21270.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13426.1; -; Genomic_DNA.
DR   PIR; F39845; F39845.
DR   RefSeq; NP_389435.1; NC_000964.3.
DR   RefSeq; WP_003232113.1; NZ_JNCM01000035.1.
DR   ProteinModelPortal; P25994; -.
DR   SMR; P25994; -.
DR   IntAct; P25994; 1.
DR   STRING; 224308.Bsubs1_010100008576; -.
DR   PaxDb; P25994; -.
DR   PRIDE; P25994; -.
DR   EnsemblBacteria; CAB13426; CAB13426; BSU15520.
DR   GeneID; 936608; -.
DR   KEGG; bsu:BSU15520; -.
DR   PATRIC; fig|224308.179.peg.1691; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   InParanoid; P25994; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   PhylomeDB; P25994; -.
DR   BioCyc; BSUB:BSU15520-MONOMER; -.
DR   BioCyc; MetaCyc:BSU15520-MONOMER; -.
DR   SABIO-RK; P25994; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001570; 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   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis;
KW   Reference proteome; Repeat.
FT   CHAIN         1   1071       Carbamoyl-phosphate synthase pyrimidine-
FT                                specific large chain.
FT                                /FTId=PRO_0000144991.
FT   DOMAIN      133    327       ATP-grasp 1.
FT   DOMAIN      671    861       ATP-grasp 2.
FT   DOMAIN      930   1071       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000250}.
FT   NP_BIND     697    754       ATP. {ECO:0000250}.
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    546       Oligomerization domain.
FT   REGION      547    929       Carbamoyl phosphate synthetic domain.
FT   REGION      930   1071       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       298    298       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       298    298       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       300    300       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       820    820       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       832    832       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       832    832       Magnesium or manganese 4. {ECO:0000250}.
FT   METAL       834    834       Magnesium or manganese 4. {ECO:0000250}.
SQ   SEQUENCE   1071 AA;  117650 MW;  195E33CFC5C6222C CRC64;
     MPKRVDINKI LVIGSGPIII GQAAEFDYAG TQACLALKEE GYEVILVNSN PATIMTDTEM
     ADRVYIEPLT PEFLTRIIRK ERPDAILPTL GGQTGLNLAV ELSERGVLAE CGVEVLGTKL
     SAIQQAEDRD LFRTLMNELN EPVPESEIIH SLEEAEKFVS QIGFPVIVRP AYTLGGTGGG
     ICSNETELKE IVENGLKLSP VHQCLLEKSI AGYKEIEYEV MRDSQDHAIV VCNMENIDPV
     GIHTGDSIVV APSQTLSDRE YQLLRNVSLK LIRALGIEGG CNVQLALDPD SFQYYIIEVN
     PRVSRSSALA SKATGYPIAK LAAKIAVGLS LDEMMNPVTG KTYAAFEPAL DYVVSKIPRW
     PFDKFESANR KLGTQMKATG EVMAIGRTLE ESLLKAVRSL EADVYHLELK DAADISDELL
     EKRIKKAGDE RLFYLAEAYR RGYTVEDLHE FSAIDVFFLH KLFGIVQFEK ELKANAGDTD
     VLRRAKELGF SDQYISREWK MKESELYSLR KQAGIAPVFK MVDTCAAEFE SETPYFYSTY
     EEENESVVTD KKSVMVLGSG PIRIGQGVEF DYATVHSVWA IKQAGYEAII VNNNPETVST
     DFSISDKLYF EPLTIEDVMH IIDLEQPMGV VVQFGGQTAI NLADELSARG VKILGTSLED
     LDRAEDRDKF EQALGELGVP QPLGKTATSV NQAVSIASDI GYPVLVRPSY VLGGRAMEIV
     YHEEELLHYM KNAVKINPQH PVLIDRYLTG KEIEVDAVSD GETVVIPGIM EHIERAGVHS
     GDSIAVYPPQ SLTEDIKKKI EQYTIALAKG LNIVGLLNIQ FVLSQGEVYV LEVNPRSSRT
     VPFLSKITGI PMANLATKII LGQKLAAFGY TEGLQPEQQG VFVKAPVFSF AKLRRVDITL
     GPEMKSTGEV MGKDSTLEKA LYKALIASGI QIPNYGSVLL TVADKDKEEG LAIAKRFHAI
     GYNILATEGT AGYLKEASIP AKVVGKIGQD GPNLLDVIRN GEAQFVINTL TKGKQPARDG
     FRIRRESVEN GVACLTSLDT AEAILRVLES MTFRADQMPA VNTNQEAAVT I
//
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