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Database: UniProt
Entry: Q75D66
LinkDB: Q75D66
Original site: Q75D66 
ID   CARB_ASHGO              Reviewed;        1113 AA.
AC   Q75D66;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   29-OCT-2014, entry version 77.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, ammonia chain;
GN   Name=CPA2; OrderedLocusNames=ABR157W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 127.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- COFACTOR: Binds 3 manganese ions per subunit. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two
CC       pathway-specific (arginine and pyrimidine) under separate control.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00409}.
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DR   EMBL; AE016815; AAS50929.2; -; Genomic_DNA.
DR   RefSeq; NP_983105.2; NM_208458.2.
DR   STRING; 33169.AGOS_ABR157W; -.
DR   PRIDE; Q75D66; -.
DR   GeneID; 4619215; -.
DR   KEGG; ago:AGOS_ABR157W; -.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234583; -.
DR   InParanoid; Q75D66; -.
DR   KO; K01955; -.
DR   OrthoDB; EOG7XPZDV; -.
DR   UniPathway; UPA00068; UER00171.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF02787; CPSase_L_D3; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN         1   1113       Carbamoyl-phosphate synthase arginine-
FT                                specific large chain.
FT                                /FTId=PRO_0000145088.
FT   DOMAIN      154    346       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      693    888       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     174    229       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     321    371       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       303    303       Manganese 1. {ECO:0000250}.
FT   METAL       317    317       Manganese 1. {ECO:0000250}.
FT   METAL       317    317       Manganese 2. {ECO:0000250}.
FT   METAL       319    319       Manganese 2. {ECO:0000250}.
FT   METAL       843    843       Manganese 3. {ECO:0000250}.
FT   METAL       859    859       Manganese 3. {ECO:0000250}.
SQ   SEQUENCE   1113 AA;  121608 MW;  8BEFC88D7C098540 CRC64;
     MSTAGISDEA SASAFTTAGY CPQLIKGIDS VLIIGSGGLS IGQAGEFDYS GSQAIKALKE
     TGKRTILINP NIATNQTSYS LADEVYFLPV TPEFITHVIK RERPDGILLT FGGQTGLNCG
     VALQRAGTLE KYGVTVLGTP ISVLETTEDR ELFARALKEI NMPIAESVAC STVEDAVAAA
     NDIGYPVIVR SAYALGGLGS GFADDDLQLR QLCAQSLALS PQVLVEKSLK GWKEIEYEVV
     RDRVGNCITV CNMENFDPLG IHTGDSIVLA PSQTLSDEEF HMLRTAAIEI IRHLGVVGEC
     NVQYALQPDG LAFKVIEVNA RLSRSSALAS KATGYPLAYT AAKIALGYTL PELPNPVTKS
     TVANFEPSLD YIVAKVPRWD LSKFQHVDKT IGSAMKSVGE VMAIGRNFEE AFQKAFRQVD
     PSLLGFQGSD EFADLDEALQ FPTDRRWLAV GEALMNRGYS VERVHELTKI DRFFLHKCMN
     IVRMQKQLET LGSINRLDEV LLRKAKKLGF CDKQIARAIS DDLSELDIRA LRKSFGILPF
     VKRIDTMAAE VPAVTNYLYV TYNAVKDDVT FGDNGIMVLG SGVYRIGSSV EFDWCAVNTV
     QALRKEGHKT IMINYNPETV STDFDEVDRL YFEELSFERV MDIYEAECAS GCVISMGGQQ
     PQNIASQLYE QGANILGTSP EDIDKAEDRH KFSTILDTLG LDQPRWSELK SLSEVKHFLD
     DVGYPVLVRP SYVLSGAAMS TVYNSEDLEG VFESAVAVSP EHPVVISKFI EGAQELDIDA
     VAYKGSLLVH AISEHVENAG VHSGDATLVL PPQSLKEEEK TRLKQLAAQV AAAWNITGPF
     NMQIIKTAEG GHTCLKIIEC NIRASRSFPF VSKVLGVNFV EIAVKAFLGG DLVPPSCDLM
     ARSYNYVATK CPQFSFTRLP GADPFLGVEM ASVGEVAAFG SNALESYWVA LQGLMSFCVP
     LPPSGILLGG DLSKEHLGRV AALLAPHGFT LLALSEATCE YLSRYLPAES SVTVLQMPET
     GREVRALFEQ HNVQCVVNLA ARRASSPIDP DYRIRRSAID FAVPLFNEPQ TTMLFARALS
     AYLPAELEMR QSDGPETPSY VLPWREYLGF KPT
//
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