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Database: UniProt
Entry: Q469Z7
LinkDB: Q469Z7
Original site: Q469Z7 
ID   CARB_METBF              Reviewed;        1071 AA.
AC   Q469Z7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   13-FEB-2019, entry version 106.
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=Mbar_A2374;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71295.1; -; Genomic_DNA.
DR   RefSeq; WP_011307341.1; NC_007355.1.
DR   ProteinModelPortal; Q469Z7; -.
DR   SMR; Q469Z7; -.
DR   STRING; 269797.Mbar_A2374; -.
DR   EnsemblBacteria; AAZ71295; AAZ71295; Mbar_A2374.
DR   GeneID; 3626715; -.
DR   KEGG; mba:Mbar_A2374; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 911at2157; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008156; 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; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1071       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066363.
FT   DOMAIN      133    325       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      673    864       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      931   1071       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     699    756       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    540       Oligomerization domain.
FT   REGION      541    932       Carbamoyl phosphate synthetic domain.
FT   REGION      933   1071       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       296    296       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       296    296       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       298    298       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   1071 AA;  118345 MW;  15C94A8E998BFFD8 CRC64;
     MPKREDIKKV LLIGSGPITI GQAAEFDFSG SQACRSLKEE GIKVVLVNSN PATIMTDPEM
     ADSVYIEPLD AKIVEKIIEK ERPDGIIAGI GGQTGLNITS ELAEKGVFEK YGVEILGTPV
     EAIKNTEDRE LFKETMLRIG EKVPLSRAVN SLKEAEDVVD ELGLPLIVRP AYTLGGAGGG
     IARTKEELLE ITERGLRRSR INQVLIEESV LGWAEIEYEV MRDENDTCIV ICNMENIDPM
     GVHTGESAVV APSQTLSDAE HQMLRSASIK IIRALKIEGG CNIQYALKEG DYRVVEVNPR
     VSRSSALASK ATGYPIARVT AKIAIGMKLD EIINNVTKST PASFEPALDY VITKIPRWPF
     DKFTTADKTL TTAMKSTGEV MAIGRTIEES LLKAFKSLDI DNQLGNKHWD EPETKTLLKT
     PTSERLFVIF DALEKGMSVK EIFELSSINP FFISKIKRIV DMEKRIRAEE LTPELLREAK
     KMGFPDTRLA ELTGSTRQEI SDLRHKAGIL ATFKMVDTCA AEFEAATPYY YSTYEDSCET
     NATTDKKKIL ILGAGPIRIG QGIEFDYCTV HAVTALREEG IETHIINNNP ETVSTDFDTS
     DKLFFEPLTL EYVMNVIERE KPDGVLVQFG GQTSVNLAIP LKQELKRRTD LNTVILGTDP
     DDMDLAEDRE KFYILMKELG VPQPEGGYAT SHKEAIEVAK RIGFPVLVRP SYVLGGRAME
     IVYDEIDLER YMKEAVRVSH EHPILIDDFL EAASEIDVDA VCDQKDVIIG AIMEHIEEAG
     VHSGDSACVI PPQSLSPEVL DQVRDYTRKI ALALKVKGLI NIQMAEKCGK VYVLEANPRS
     SRTIPFVSKS VGIPLAKIAA KVIAGHSLKS LGYTDEPKPK HVSIKEVLLP FDKLPGADPV
     LGPEMKSTGE VMGIDYDFGR AYYKAELAAD NVLPLTGKVF LSIRNADKTE LVDVAKKLQA
     AGLELMGTEG TVNYLARHGV FMDVVKKVHD GSPNVIDMMR RDEVDLIINT PTSKQSRRDG
     SRIRRAAVDF KVPYITTMQA AIAAAAAIET MKKGEELTIK SINEYHKEME N
//
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