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Database: UniProt
Entry: C1FNY3
LinkDB: C1FNY3
Original site: C1FNY3 
ID   CARB_CLOBJ              Reviewed;        1068 AA.
AC   C1FNY3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   05-DEC-2018, entry version 63.
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=CLM_2001;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G.,
RA   Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-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; CP001581; ACO83513.1; -; Genomic_DNA.
DR   RefSeq; WP_012703727.1; NC_012563.1.
DR   ProteinModelPortal; C1FNY3; -.
DR   SMR; C1FNY3; -.
DR   PRIDE; C1FNY3; -.
DR   EnsemblBacteria; ACO83513; ACO83513; CLM_2001.
DR   KEGG; cby:CLM_2001; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   BioCyc; CBOT536232:G1GVA-1923-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001374; 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   1068       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164709.
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      933   1068       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   1068       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   1068 AA;  119061 MW;  0EE3ADE538E6C973 CRC64;
     MPLNKDIKKV LVIGSGPIVI GQAAEFDYSG TQACEGLKEE GVEVVLINSN PATIMTDKKV
     ADKVYLEPLT VEFVEKVIAK ERPDSLLAGM GGQTGLNLAV ELYDKGILKK YGVNVIGTSI
     ESIKEGEDRE LFRNVMSRIN GPVIQSEIVT DMENGKAFAN KIGYPIIVRP AYTLGGTGGG
     IAESEEELDE ILALGLQLSS IGQVLLEKSV KGWKEIEYEV MRDSRGNCIT VCNMENIDPV
     GIHTGDSIVV APSQTLSDKE YQMLRSASIN ILNSIGIKGG CNVQFALNPN SFEYAVIEIN
     PRVSRSSALA SKATGYPIAK VASKIALGYT LDEIKNAVTQ KTYACFEPSL DYVVVKIPKW
     PFDKFQGADR VLGTKMMATG EIMAIGSNFE AAFLKGTRSL EIGKYSLEHK KFRELSIEEL
     KTRVISPDDE RIFALAEMLR RDYRMDKVAE ITGIDKFFIK KFRWIVEEEQ RLRLSKIDDL
     DKEWLYKLKK KGFSDKGIAD MLKVNPEDIY RLRNIWRINP VYKMVDTCGG EFEALSPYYY
     STYDVYDEVE VSKNKKVIVI GSGPIRIGQG IEFDYASVHC VKALKKLGIE TIIVNNNPET
     VSTDFDVSDK LYFEPLTEED VLNIVEKEKP DGVILQFGGQ TAIKLANFLK EKNISTLGTT
     ADQIDMAEDR EKFDELLEKL KIARPKGKGI WSVEDGLEEA KKLGFPVLVR PSYVLGGQGM
     EITHDEKELV YYLSNAFQKD KKNPILIDKY LMGREIEVDA ISDGEDVLIP GIMEHLERAG
     VHSGDSITMY PTQNVSKDIK EKILEYTKKL ALGIGIKGMI NIQFIEFQGN LYVIEVNPRA
     SRTVPYISKV SKVPIVDIAT RVMLGEKLND LGYGVGVYKE PELISVKVPV FSTQKLPRVE
     VCLGPEMKST GEVLGVGKTL EEALYKGFIG ANMSIKKEKG TVLATINDHD KEEFLPIAKK
     LHSLGYKFIA TSKTAELLKE EGIEVKQVRK LKEESPNIID TIKNDEVDLV VNTPTKGNDS
     KRDGFHIRRA AIERNLGVIT SLDTLKAIVD IKFKEIKDET LYIFDLSN
//
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