ID CARB_BACWK Reviewed; 1072 AA.
AC A9VTC6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 05-DEC-2018, entry version 79.
DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210};
GN OrderedLocusNames=BcerKBAB4_3713;
OS Bacillus weihenstephanensis (strain KBAB4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01210};
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 {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000255|HAMAP-Rule:MF_01210}.
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 {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
DR EMBL; CP000903; ABY44882.1; -; Genomic_DNA.
DR RefSeq; WP_012261602.1; NC_010184.1.
DR ProteinModelPortal; A9VTC6; -.
DR SMR; A9VTC6; -.
DR STRING; 315730.BcerKBAB4_3713; -.
DR PRIDE; A9VTC6; -.
DR EnsemblBacteria; ABY44882; ABY44882; BcerKBAB4_3713.
DR KEGG; bwe:BcerKBAB4_3713; -.
DR eggNOG; ENOG4105CU6; Bacteria.
DR eggNOG; COG0458; LUCA.
DR HOGENOM; HOG000234583; -.
DR KO; K01955; -.
DR OMA; AVFPFNK; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000002154; Chromosome.
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 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; Repeat.
FT CHAIN 1 1072 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000138884.
FT DOMAIN 133 327 ATP-grasp 1. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 671 861 ATP-grasp 2. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 930 1072 MGS-like. {ECO:0000255|PROSITE-
FT ProRule:PRU01202}.
FT NP_BIND 159 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT NP_BIND 697 754 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT REGION 1 401 Carboxyphosphate synthetic domain.
FT REGION 402 546 Oligomerization domain.
FT REGION 547 929 Carbamoyl phosphate synthetic domain.
FT REGION 930 1072 Allosteric domain.
FT METAL 284 284 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 300 300 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 820 820 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 834 834 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ SEQUENCE 1072 AA; 118522 MW; 15D3A2DF42EC73B0 CRC64;
MPKRLDINTI LVIGSGPIVI GQAAEFDYSG TQACQSLREE GYKVILVNSN PATIMTDTAT
ADKVYIEPLT LEFVSRIIRK ERPDALLPTL GGQTGLNMAV ELAKSGILEE CGVEILGTKL
SAIEQAEDRD LFRTLMQELN EPIPSSTIIH TLEEAHEFVK EIGYPVIVRP AFTMGGTGGG
ICNNEEELIE IVSGGLKHSP VTQCLLEKSI AGCKEIEYEV MRDSNDNAIV VCNMENIDPV
GVHTGDSIVV APSQTLSDRE YQMLRNTSLR IIRALGIEGG CNVQLALDPH SFQYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEIINPVTQ KTYACFEPAL DYVVSKIPRW
PFDKFESANR TLGTQMKATG EVMSIGRNLE QSLLKAIRSL ELGVYHLELD HLKELDKETM
KKRIIKADDE RLFVVAEAIR QGVTKEEINE WCEMDFFFLQ KVENIVNMER EVKANVGNME
VLQAAKEMGF SDHYIANAWN KTEREIYDMR KESNMTPVYK MVDTCAAEFE SATPYYYSTY
GDENESIVTD RKSVVVLGSG PIRIGQGVEF DYATVHSVWA IKEAGYEAII VNNNPETVST
DFSISDKLYF EPLTIEDVMH IIDLEKPEGV IVQFGGQTAI NLAAKLEAHG VKILGTSLED
LDRAEDRDKF EAALTKLGIP QPVGKTATTV EQAVAIADKI GYPVLVRPSY VLGGRAMEIV
YRQEELLHYM KNAVKVHADH PVLIDRYMVG KEIEVDAISD GENVFIPGIM EHIERAGVHS
GDSIGVYPPQ SLSEKLKEQI IEHTIGLGKG LNIVGLLNIQ FVVFKDEVYV IEVNPRASRT
VPFLSKITGV PMANIATKVI LGQNLVEQGY GTGYHPEEKE VYVKAPVFSF AKLRSVDTTL
GPEMKSTGEV MGKDLTLEKA LYKGLVASGI NIPTHGSVII TVADKDKEEA LEIAKRFHEI
GYNLLATAGT AQSLTEQNIP VQVVNKIDSE DYNLLDIIRQ GKAQFVINTL TKGKQPARDG
FRIRRESVEN GVACLTSLDT TRAILRVLES MTFSAHSMKE ITQTKRHEVV HA
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