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 01-MAY-2013, entry version 71.
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 SEQUENCE REVISION TO 127.
RA Dietrich F.S., Voegeli S., Philippsen P.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
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 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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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 KO; K01955; -.
DR OMA; SSPTAYM; -.
DR OrthoDB; EOG4T7CBC; -.
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: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; 2.
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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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.
FT DOMAIN 693 888 ATP-grasp 2.
FT NP_BIND 174 229 ATP (Potential).
FT NP_BIND 321 371 ATP (Potential).
FT METAL 303 303 Manganese 1 (By similarity).
FT METAL 317 317 Manganese 1 (By similarity).
FT METAL 317 317 Manganese 2 (By similarity).
FT METAL 319 319 Manganese 2 (By similarity).
FT METAL 843 843 Manganese 3 (By similarity).
FT METAL 859 859 Manganese 3 (By similarity).
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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