CARB_ASHGO
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 03-AUG-2022, entry version 112.
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 Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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 Saccharomyces
RT 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:
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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC 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 the
CC 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 pathway-
CC specific (arginine and pyrimidine) under separate control.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50929.2; -; Genomic_DNA.
DR RefSeq; NP_983105.2; NM_208458.2.
DR AlphaFoldDB; Q75D66; -.
DR SMR; Q75D66; -.
DR STRING; 33169.AAS50929; -.
DR EnsemblFungi; AAS50929; AAS50929; AGOS_ABR157W.
DR GeneID; 4619215; -.
DR KEGG; ago:AGOS_ABR157W; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR InParanoid; Q75D66; -.
DR OMA; IEPAGIH; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
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:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
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; 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; Cytoplasm;
KW Ligase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1113
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000145088"
FT DOMAIN 154..346
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 693..888
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 957..1113
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT BINDING 174..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 321..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 843
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 859
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="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
