ID   CARA_NEUCR              Reviewed;         453 AA.
AC   P22572; Q7RVF2; V5IMB9;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 156.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain, mitochondrial;
DE            Short=CPS-A;
DE            EC=6.3.5.5;
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain;
DE   Flags: Precursor;
GN   Name=arg-2; Synonyms=cpa1; ORFNames=NCU07732;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2141606; DOI=10.1016/s0021-9258(19)38545-x;
RA   Orbach M.J., Sachs M.S., Yanofsky C.;
RT   "The Neurospora crassa arg-2 locus. Structure and expression of the gene
RT   encoding the small subunit of arginine-specific carbamoyl phosphate
RT   synthetase.";
RL   J. Biol. Chem. 265:10981-10987(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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: Mitochondrion matrix.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33609.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; J05512; AAA33609.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CM002239; ESA42831.1; -; Genomic_DNA.
DR   EMBL; CM002239; ESA42832.1; -; Genomic_DNA.
DR   PIR; A42224; A42224.
DR   RefSeq; XP_011394270.1; XM_011395968.1.
DR   RefSeq; XP_011394271.1; XM_011395969.1.
DR   AlphaFoldDB; P22572; -.
DR   SMR; P22572; -.
DR   STRING; 5141.EFNCRP00000008065; -.
DR   EnsemblFungi; ESA42831; ESA42831; NCU07732.
DR   EnsemblFungi; ESA42832; ESA42832; NCU07732.
DR   GeneID; 3878130; -.
DR   KEGG; ncr:NCU07732; -.
DR   VEuPathDB; FungiDB:NCU07732; -.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   InParanoid; P22572; -.
DR   OMA; CFNTGMT; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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; Ligase;
KW   Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT   CHAIN           46..453
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain, mitochondrial"
FT                   /id="PRO_0000004222"
FT   DOMAIN          233..420
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          26..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  49355 MW;  1C178675F213DBA5 CRC64;
     MFSRLAARLP KASALNGVAA RQVRNLSQPA ITGSKGRNMP AREPRTTAAA TGAEATFTIR
     DGPVFQGTAF GANTNISGEA VFTTSLVGYP ESMTDPSYRG QILVFTQPLI GNYGVPSNER
     DEFNLLKYFE SPHIQCAGIV VSDVATQYSH WTAVQSLGEW CASEGIPAIS GVDTRAIVTY
     LREQGSSLAR ISIGDEYDAD EDEGFIDPGQ INLVKRVSTK APFVVTNPNA KFHVALIDCG
     VKENILRSLV SRGASVTVFP YNYPIHKVAE NFDGVFISNG PGDPTHCQET VYNLAKLMET
     SPIPIMGICL GHQLLALAVG AKTIKLKYGN RAHNIPALDL TTGQCHITSQ NHGYAVDIST
     LPSDFKEYFV NLNDGSNEGM MHKTRPIFST QFHPEAKGGP MDSSYLFDKY MENVELFKSN
     SQVYRDNRPT QFMIDILSKE RVGVEPTPLS NAA