ID   CARA_HYPVI              Reviewed;         453 AA.
AC   P87183;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE            Short=CPS-A;
DE            EC=6.3.5.5;
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain;
GN   Name=cpa1; Synonyms=arg2;
OS   Hypocrea virens (Gliocladium virens) (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=29875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9501476; DOI=10.1006/fgbi.1997.1025;
RA   Baek J.M., Kenerley C.M.;
RT   "The arg2 gene of Trichoderma virens: cloning and development of a
RT   homologous transformation system.";
RL   Fungal Genet. Biol. 23:34-44(1998).
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   -!- 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   -!- 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 CarA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF001029; AAB58299.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87183; -.
DR   SMR; P87183; -.
DR   UniPathway; UPA00068; UER00171.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding.
FT   CHAIN           1..453
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000004223"
FT   DOMAIN          233..420
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        309
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  49434 MW;  39B644DE774F0CAA CRC64;
     MFSKLAANFA QRAAGSAAGT TRRVAFQTRF VSSQTLANGS KGRAIPFQKP GSVPATFTIR
     DGPVFRGKAF GANANISGEA VFTTSLVGYP ESMTDPSYRG QILVFTQPLI GNYGVPSNER
     DEYNLLKYFE SPHIQCAGVV VSDVALNYSH WTAVESLSEW CAREASPPSP ASDTRAIVTH
     LREQGSSLAR ISIGDEYDAD EDESFVDPGQ INLVKRVSTK APFVIESPGA DLHVALIDCG
     VKENILRQLV SRGASLTVFP YNYPIHKVAD HFDGVFISNG PGDPIHCQET VYNLARLMET
     SSIPIMGICL GHQLLAMAVG AKTIKMKYGN RAHNIPALDL TTGQCHITSQ NHGYAVDAST
     LPNDFKEYFV NLNDGSNEGM MHRTRPIFST QFHPEAKGGP MDSSYLFEKY LENVRAAKSA
     QRVYKDNRPS QYVLDVLSKE RVGVEPVPLV GFA