GenomeNet

Database: UniProt
Entry: A5UKG5
LinkDB: A5UKG5
Original site: A5UKG5 
ID   CARB_METS3              Reviewed;        1058 AA.
AC   A5UKG5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JAN-2019, entry version 74.
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=Msm_0488;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 /
OS   PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M.,
RA   Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K.,
RA   Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to
RT   the human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86693.1; -; Genomic_DNA.
DR   RefSeq; WP_004032238.1; NC_009515.1.
DR   ProteinModelPortal; A5UKG5; -.
DR   SMR; A5UKG5; -.
DR   STRING; 420247.Msm_0488; -.
DR   PRIDE; A5UKG5; -.
DR   EnsemblBacteria; ABQ86693; ABQ86693; Msm_0488.
DR   GeneID; 5217279; -.
DR   KEGG; msi:Msm_0488; -.
DR   PATRIC; fig|420247.28.peg.486; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001992; 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   1058       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066367.
FT   DOMAIN      131    325       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      663    856       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      923   1058       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     157    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     689    746       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    538       Oligomerization domain.
FT   REGION      539    924       Carbamoyl phosphate synthetic domain.
FT   REGION      925   1058       Allosteric domain.
FT   METAL       282    282       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       813    813       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       827    827       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       827    827       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       829    829       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1058 AA;  116693 MW;  EB5FD1FDDBD362C4 CRC64;
     MPIDKDIKKV LIIGSGPIQI GQAAEFDYSG SQACKSLREE GIETVLVNSN PATIQTDMDM
     ADTVYTEPLT PEIVSEIIKK ENVDAILPTM GGQTGLNIAT GLGDLGLLDG IKVLGSDIQT
     IKDVEDRDLF GHFMDKLNEP IPKCHAVESV EEAIEAVKDI GYPVIVRPAF TLGGTGGGVA
     YNEEELIEIA THGLDMSFIN QVLIDESVLG WKEFEYEVMR DKEDTCIIVC NMENIDPMGI
     HTGESVVVAP AQNLNDRDSQ ALRDASIKII RALGIQGGCN IQFAVNPETG EYKVIEVNPR
     VSRSSALASK ATGYPIAKIS SKIALGMTLD EIKNDITKET PASFEPAIDY VVVKIPRWPF
     DKFRGINREI GVQMKATGEV MAIGRTFEEA IQKAIRSLDM GHDGFEYVEY TEDDLANPTD
     ERLFQLYSAI KDGMDLDKIQ KLTNIDKFFL YKIRNIVNFE NEVTEEKLND ADFLRKAKQM
     GCSNKRLAAL SNQTEEYIRN LLNRFNIKQS YKMVDTCAAE FEAKTPYYYS TYDSGNELKS
     SNKKKIVILG AGPIRIGQGI EFDYCCVHSS LALKDEGIET ILINNNPETV STDYDISDKL
     FFEPITFEDV MGIIDQEKPD GVIVQFGGQT SINLAVPLAN AGVKILGTPY ESIDGVEDRE
     LFAKLLNKLH IHQAPYGTAN SFEEAREIAE RITFPVLVRP SYVIGGRAME IVYDNNELEK
     YMKEAVKVSP EHPILVDKFL EDAIELDVDV LCDGEEVFIA GIMEHIEEAG VHSGDSACVI
     PPQTIPEHIL NTIREYSTKL ALELDVKGLM NIQYAVKLDE EMVYIIEANP RASRTVPFVS
     KAIGVPLAKV ATWIMTGAKL KDFNLTKEIK IDHVAVKESV FPFLKLPESD TVLGPEMKST
     GESIGVDENF GMAFYKSQLA AGMDLPKEGK IFISVKEQDK KKIRPIAEKA ANLGFELAAT
     SGTADAAKGV DIEKIKKVSQ GSPNIRDAIL NKEIDLIINT SEGKQSAQDG YIIRRLAIEL
     GIPYVTTLSG ARAALNAIEA VQNNEITVKS LNEHIDGE
//
DBGET integrated database retrieval system