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Database: UniProt
Entry: B2UX86
LinkDB: B2UX86
Original site: B2UX86 
ID   CARB_CLOBA              Reviewed;        1069 AA.
AC   B2UX86;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=CLH_0055;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska
RT   E43.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001078; ACD52312.1; -; Genomic_DNA.
DR   RefSeq; WP_012450483.1; NC_010723.1.
DR   ProteinModelPortal; B2UX86; -.
DR   SMR; B2UX86; -.
DR   PRIDE; B2UX86; -.
DR   EnsemblBacteria; ACD52312; ACD52312; CLH_0055.
DR   KEGG; cbt:CLH_0055; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; CBOT508767:G1GC0-52-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
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; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1069       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000138886.
FT   DOMAIN      133    327       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      674    864       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      932   1069       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     700    757       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    549       Oligomerization domain.
FT   REGION      550    932       Carbamoyl phosphate synthetic domain.
FT   REGION      933   1069       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       823    823       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       837    837       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1069 AA;  119182 MW;  510218DF245B466B CRC64;
     MPLNKDIKRV LVIGSGPIVI GQAAEFDYSG TQACEALKSE GVEVVLINSN PATIMTDKEV
     ADKVYLEPLT LEFIEKVIAK EKPDSLLAGM GGQTGLNLAV ELHDAGILDK YNVKVIGTSI
     ESIKEGEDRE LFRDMMNRIG EPVIKSEIVT DLQAGIDFAN KIGYPVIVRP AYTLGGSGGG
     IADDEEELRT ILESGLQLST IGQVLLEKSV KGWKEIEYEV MRDSYGNCIT VCNMENIDPV
     GIHTGDSIVV APSQTLSDKE YQMLRTASIN IINAVGIEGG CNVQFSLNPN TFEYAVIEIN
     PRVSRSSALA SKATGYPIAK LAAKIALGYG LDEIKNAVTQ KTYACFEPTL DYVVVKIPKW
     PFDKFFGADR QLGTKMMATG EIMAIGANFE QAFLKGIRSL EIGKYSLDHK KFKEHSMSEL
     KDLVMKPDDE RIFALAEMLR RDYMIERINK ITGIDKFFLE KIKWIVEEEQ RLKLSNIEDL
     DKEWLKNLKK KGFSDKAIAD MLKVSPEDIY RLRDIWSIKP SYKMVDTCGG EFEALSPYYY
     STYEQYDEVE VSNRRKVIVI GSGPIRIGQG IEFDYASVHC VKALKKLDIE TIIVNNNPET
     VSTDFDISDK LYFEPLTEED VLNIIEKENP YGVILQFGGQ TAIKLANFLK EKNIKTLGTT
     ADQIDMAEDR EKFDELLERL DISRPKGKGI WSVEEGLEEA ERLGFPVLVR PSYVIGGQGM
     EITHDEEELT FYLTNAFAKD KKNPILIDKY LMGREIEVDA ISDGENILIP GIMEHLERAG
     VHSGDSVTMY PSQNVCDKIK GKILEYTKKL ALAIGIKGMI NIQFIEFEGS LYVIEVNPRA
     SRTVPYISKV SGVPIVDIAT QVMLGAKLND LGYGVDIYKE PELISVKVPV FSTQKLPNVE
     VCLGPEMRST GEVLGVGRTL KEALYKGFVG ANMYPSKEKG KILATINKHN KAEFLPIAKD
     LAKVGYKFIA TTGTCKLLRD EGIDAEEIRK IDEEKPNILD IVKNREVDLV VNTPTKGNDS
     KRDGFLIRRA AVERNLGVIT ALDTLRAIAD VELEEFDKNK DLEVFDITK
//
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