CARY_BACSU
ID CARY_BACSU Reviewed; 1030 AA.
AC P18185;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; Synonyms=cpaB; OrderedLocusNames=BSU11240;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8025667; DOI=10.1099/13500872-140-5-1023;
RA O'Reilly M., Devine K.M.;
RT "Sequence and analysis of the citrulline biosynthetic operon argC-F from
RT Bacillus subtilis.";
RL Microbiology 140:1023-1025(1994).
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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP SEQUENCE REVISION TO 397; 510 AND 626.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 873-1030.
RC STRAIN=168 / EMG50;
RX PubMed=2117745; DOI=10.1093/nar/18.15.4594;
RA Mountain A., Smith M.C.M., Baumberg S.;
RT "Nucleotide sequence of the Bacillus subtilis argF gene encoding ornithine
RT carbamoyltransferase.";
RL Nucleic Acids Res. 18:4594-4594(1990).
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; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z26919; CAA81548.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12965.3; -; Genomic_DNA.
DR EMBL; X53360; CAA37443.1; ALT_INIT; Genomic_DNA.
DR PIR; I40377; I40377.
DR RefSeq; NP_389006.3; NC_000964.3.
DR RefSeq; WP_003232982.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P18185; -.
DR SMR; P18185; -.
DR IntAct; P18185; 1.
DR MINT; P18185; -.
DR STRING; 224308.BSU11240; -.
DR PaxDb; P18185; -.
DR PRIDE; P18185; -.
DR EnsemblBacteria; CAB12965; CAB12965; BSU_11240.
DR GeneID; 939353; -.
DR KEGG; bsu:BSU11240; -.
DR PATRIC; fig|224308.179.peg.1209; -.
DR eggNOG; COG0458; Bacteria.
DR InParanoid; P18185; -.
DR OMA; TKMKATG; -.
DR PhylomeDB; P18185; -.
DR BioCyc; BSUB:BSU11240-MON; -.
DR SABIO-RK; P18185; -.
DR UniPathway; UPA00068; UER00171.
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: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 GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; SSF48108; 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; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1030
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000144992"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT DOMAIN 675..863
FT /note="ATP-grasp 2"
FT DOMAIN 925..1027
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..548
FT /note="Oligomerization domain"
FT REGION 549..928
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 929..1030
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 701..756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CONFLICT 397
FT /note="A -> G (in Ref. 1; CAA81548)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="A -> R (in Ref. 1; CAA81548)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="A -> R (in Ref. 1; CAA81548)"
FT /evidence="ECO:0000305"
FT CONFLICT 854..857
FT /note="MIPL -> R (in Ref. 1; CAA81548)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="G -> A (in Ref. 5; CAA37443)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="A -> R (in Ref. 5; CAA37443)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="F -> S (in Ref. 5; CAA37443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 112798 MW; 73508761F7E25C9E CRC64;
MPKDTSISSI LVIGSGPIII GQAAEFDYSG TQGCIALKEE GYRVILVNSN PATIMTDEAF
ADEIYFEPLT AESLTAIIKK ERPDGLLANL GGQTALNLAV ELEETGVLKE HGVKLLGTSV
ETIQKGEDRE KFRSLMNELK QPVPESEIVD NEADALHFAE SIGFPVIIRP AYTLGGKGGG
IAPDKEAFTA MIKQALLASP INQCLVEKSI AGFKEIEYEV MRDSNNTCIT VCNMENIDPV
GVHTGDSIVV APSQTLTDED YQMLRTASLT IISALDVVGG CNIQFALDPF SKQYYVIEVN
PRVSRSSALA SKATGYPIAK MAAKLAVGYT LDELKNPLTG STYASFEPAL DYVIVKFPRW
PFDKFKNADR KLGTKMKATG EVMAIERNLE AAIQKAAASL ELKNIGTHLP ELSGLSIDTL
WDLAITPDDR RFFVVMELLS RSVSIDDIHE KTKIDPFFLH TFDNIIKLEN RLMEAGSDLS
FELLKKAKEK GFSDATIASL ISKTEEEVRA LRKEMGITPS FKIVDTCAAE FDAKTNYFYS
TYFGETDGDI SRKEKKRALI IGSGPIRIGQ GVEFDYSAVH GVLTLQELGF ETIMINNNPE
TVSTDYEIAD RLYFEPMTTE HIVNVAEQEN IDFAIVQFGG QTAINAAEAL EKAGITLLGT
SFQTLDVLED RDQFYQLLDE LGLKHAKGEI AYTKEEAASK ASEIGYPVLI RPSYVIGGMG
MIIVDSQAQL SQLLNDEDSM PYPILIDQYV SGKEVEIDLI SDGEEVFIPT YTEHIERAGV
HSGDSFAILP GPSITSGLQQ GMKDAAQKIA RKLSFKGIMN IQFVIDNGNI LVLEVNPRAS
RTVPVVSKVM GVPMIPLATR LLAGASLKDL NPAVQNHHGV AVKFPVFSSH AIQDVDVKLG
PEMKSTGEGM CVAYDSNSAL KKIYTRVWSQ KGSIYLQNVP EDVKELAENA GFTIHEGTFA
SWMEQEGNSL HINLSGSEEA RKERLEAMTH GIPVFTEEET VRAFLQSGSG HPQPVSLKDL
YKKEVASCTQ
