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Database: UniProt
Entry: A6LPD9
LinkDB: A6LPD9
Original site: A6LPD9 
ID   CARB_CLOB8              Reviewed;        1069 AA.
AC   A6LPD9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   16-JAN-2019, entry version 82.
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=Cbei_0029;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L.,
RA   Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W.,
RA   Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H.,
RA   Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) 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; CP000721; ABR32219.1; -; Genomic_DNA.
DR   RefSeq; WP_011967394.1; NC_009617.1.
DR   ProteinModelPortal; A6LPD9; -.
DR   SMR; A6LPD9; -.
DR   STRING; 290402.Cbei_0029; -.
DR   PRIDE; A6LPD9; -.
DR   EnsemblBacteria; ABR32219; ABR32219; Cbei_0029.
DR   KEGG; cbe:Cbei_0029; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; CBEI290402:G1G93-39-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000565; 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   1069       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000085556.
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;  118811 MW;  B36C07126186C906 CRC64;
     MPLNKDIKKV LVIGSGPIVI GQAAEFDYSG TQACEALKSE GIEVVLVNSN PATIMTDKEV
     ADKVYLEPLT LEFVEKVIAK ERPDSLLAGM GGQTGLNLAV ELHDSGILEK YNVKVIGTSI
     ASIKEGEDRE LFRDMMNRIG EPVIKSEIVT DLTAGLEFAN KIGYPVIVRP AYTLGGSGGG
     IADDEEQLRT ILESGLQLST IGQVLLEKSV KGWKEVEYEV MRDSYGNCIT VCNMENIDPV
     GIHTGDSIVV APSQTLSDKE YQMLRTASIN IINAVGIEGG CNVQFSLNPN SFEYAVIEIN
     PRVSRSSALA SKATGYPIAK LAAKIALGYG LDEIKNAVTQ KTYACFEPTL DYVVVKIPKW
     PFDKFFGADR ELGTKMMATG EIMAIGANFE QAFLKGIRSL EIGKYSLDHN KFKEYSISKL
     KSIVMKPDDE RIFALAEMIR RDYMIDRINK ITGIDMFFLE KIKWIVEEEQ RLKLSKIEDL
     DKEWLHHLKK KGFSDKAIAD MLKVSPDDVY RLRDIWSIKP SYKMVDTCGG EFEALSPYYY
     STYEQYDEVE VSNNKKVIVI GSGPIRIGQG IEFDYASVHC VKALKKLGIE TIIVNNNPET
     VSTDFDVSDK LYFEPLTEED VLNIIEKEKP DGVILQFGGQ TAIKLANFLK EQNIVTLGTT
     ADQIDMAEDR EKFDELLERL GISRPKGKGI WSLEEGLEEA KRLKFPVLVR PSYVIGGQGM
     EITHDEEELT YYLENAFAKD SKNPILIDKY LMGREIEVDA ISDGENILIP GIMEHLERAG
     VHSGDSVTMY PSQNISDKIK ADVLEYTKKL ALAIGIKGMI NIQFIEFEGE LYVIEVNPRA
     SRTVPYISKV SGVPIVDLAT QVMLGAKLKE LGYGIDVYKE PELVSVKVPV FSTQKLPNVE
     VSLGPEMRST GEVLGVGRNI KEALYKGFVG AYMYPSKEKG KILATINKHD KAEFLPIAKD
     LASVGYKFIA TSGTCALLKE AGIEVEEIRK IDEEEPNILD IVKNREVDLV VNTPTKGNDS
     KRDGFLIRRA AVERNLGVIT ALDTLRAIAD VELEKFDENK DLEVFNIAK
//
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