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Database: UniProt
Entry: Q827Q7
LinkDB: Q827Q7
Original site: Q827Q7 
ID   CARB_STRAW              Reviewed;        1102 AA.
AC   Q827Q7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JAN-2019, entry version 112.
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=SAV_6867;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC74578.1; -; Genomic_DNA.
DR   RefSeq; WP_010988265.1; NZ_JZJK01000082.1.
DR   ProteinModelPortal; Q827Q7; -.
DR   SMR; Q827Q7; -.
DR   STRING; 227882.SAV_6867; -.
DR   PRIDE; Q827Q7; -.
DR   EnsemblBacteria; BAC74578; BAC74578; SAVERM_6867.
DR   KEGG; sma:SAVERM_6867; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; SAVE227882:G1G23-7184-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000428; 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_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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1102       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145049.
FT   DOMAIN      138    334       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      682    873       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      955   1100       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     165    222       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     708    765       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    408       Carboxyphosphate synthetic domain.
FT   REGION      409    553       Oligomerization domain.
FT   REGION      554    954       Carbamoyl phosphate synthetic domain.
FT   REGION      955   1102       Allosteric domain.
FT   METAL       291    291       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       305    305       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       305    305       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       307    307       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       832    832       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       844    844       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       844    844       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       846    846       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1102 AA;  117894 MW;  30E31E42A66033B3 CRC64;
     MPKRTDIQSV LVIGSGPIVI GQAAEFDYSG TQACRILRAE GLRVILVNSN PATIMTDPEI
     ADATYVEPIT PEFVEKIIAK ERPDALLPTL GGQTALNTAI SMHEQGVLEK YGVELIGANV
     EAINKGEDRD LFKGVVEAVR AKIGHGESAR SVICHSMDDV LEGVETLGGY PVVVRPSFTM
     GGAGSGFAHD EEELRRIAGQ GLTLSPTTEV LLEESILGWK EYELELMRDK NDNVVVVCSI
     ENFDPMGVHT GDSITVAPSM TLTDREYQRL RDIGIAIIRE VGVDTGGCNI QFAVNPDDGR
     IIVIEMNPRV SRSSALASKA TGFPIAKIAA KLAVGYTLDE IPNDITEKTP ASFEPTLDYV
     VVKAPRFAFE KFPSADSTLT TTMKSVGEAM AIGRNFTEAL QKALRSLEKK GSQFTFVGEP
     GDKALLLEEA VRPTDGRINS VMQAIRAGAT PEEVFEATKI DPWFVDQLFL IKELADELAA
     ADKLDPELLA EAKRHGFSDV QIAEIRGLRE DVVREVRHAL GVRPVYKTVD TCAAEFAAKT
     PYFYSSYDEE SEVAPREKPA VIILGSGPNR IGQGIEFDYS CVHASFALSE AGYETVMVNC
     NPETVSTDYD TSDRLYFEPL TLEDVLEIVH AETLAGPVAG VIVQLGGQTP LGLSQALKDN
     GVPVVGTPPE AIHAAEDRGA FGQVLAEAGL PAPKHGTATT FAGAKAIADE IGYPVLVRPS
     YVLGGRGMEI VYDETRLESY IAESTEISPS RPVLVDRFLD DAIEIDVDAL YDGEELYLGG
     VMEHIEEAGI HSGDSACALP PITLGGFDIK RLRASTEAIA KGVGVRGLIN IQFAMAGDIL
     YVLEANPRAS RTVPFTSKAT AVPLAKAAAR ISLGATIAEL RAERLLPANG DGGTLPLDAP
     ISVKEAVMPW SRFRDIHGRG VDTVLGPEMR STGEVMGIDS VFGTAYAKSQ AGAYGPLPTK
     GRAFISVANR DKRSMIFPAR ELVAHGFELL ATSGTAEVLK RNGINATVVR KQSEGEGPGG
     EKTIVQLIHD GQVDLIVNTP YGTGGRLDGY EIRTAAVARS VPCLTTVQAL AAAVQGIDAL
     THGDVGVRSL QEHAEHLTAA RD
//
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