ID   CARA_CHAGB              Reviewed;         461 AA.
AC   Q2H132;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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; ORFNames=CHGG_04514;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR   EMBL; CH408032; EAQ87895.1; -; Genomic_DNA.
DR   RefSeq; XP_001223728.1; XM_001223727.1.
DR   AlphaFoldDB; Q2H132; -.
DR   SMR; Q2H132; -.
DR   STRING; 38033.XP_001223728.1; -.
DR   EnsemblFungi; EAQ87895; EAQ87895; CHGG_04514.
DR   GeneID; 4392718; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   InParanoid; Q2H132; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 566537at2759; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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; Reference proteome.
FT   CHAIN           1..461
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000290592"
FT   DOMAIN          240..427
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  50215 MW;  733A877682E9348A CRC64;
     MSFFFSRQSD ISFLLFSEST STTRNSSQAR LLSRLAVDGS KGRAMPVLNT TRATAAASGV
     DATLTIRDGP VFHGTAFGAN SNISGEAVFT TSLVGYPESM TDPSYRGQIL VFTQPLIGNY
     GVPSNQRDEY GLLKYFESPH IQCAGVVVAD VAEKYSHWTA VESLSEWCAR EGVPVISGVD
     TRAIVTHLRE QGSSLARISI GDEYDADEDE GFIDPGAINL VKRVSTKAPF VVSNPNATFH
     VALIDCGVKE NILRSLVSRG ASVTVFPYNY PIHKVADNFD GVFISNGPGD PTHCQETVYN
     LGRLMETSSV PIMGICLGHQ LLALAVGAQT IKLKYGNRAH NIPALDLTTG QCHITSQNHG
     YAVDASTLPS EFKEYFVNLN DGSNEGMMHK TRPIFSTQFH PEAKGGPMDS SYLFDKYLEN
     VQMYKDNSKV YRDNRPSQLM IDILSKERVG VEPSPLAANA I