ID   CARA_PHANO              Reviewed;         476 AA.
AC   Q0U5H7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=SNOG_12987;
OS   Phaeosphaeria nodorum (Septoria nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Phaeosphaeriaceae;
OC   Phaeosphaeria.
OX   NCBI_TaxID=13684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from HCO(3)(-): 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   -!- SIMILARITY: Belongs to the carA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; CH445348; EAT79787.1; -; Genomic_DNA.
DR   RefSeq; XP_001803201.1; -.
DR   GeneID; 5980114; -.
DR   OMA; Q0U5H7; EGVPAIS.
DR   BRENDA; 6.3.5.5; 281328.
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-hyd...; IEA:EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11405:SF4; CarA_synth_small; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
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;
KW   Complete proteome; Cytoplasm; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    476       Carbamoyl-phosphate synthase arginine-
FT                                specific small chain.
FT                                /FTId=PRO_0000290598.
FT   DOMAIN      228    415       Glutamine amidotransferase type-1.
FT   ACT_SITE    304    304       Nucleophile (By similarity).
FT   ACT_SITE    388    388       By similarity.
FT   ACT_SITE    390    390       By similarity.
SQ   SEQUENCE   476 AA;  52138 MW;  AEBD2D76D5F792E3 CRC64;
     MFSHLLKPAA RSAGLLGHVN RRYLATVHTN TAREIPKPSR KPTPISLENA TFTIKNGPIF
     SGKSFGAKAN ISGEAVFTTS LVGYPESMTD PSYRGQILVF TQPLIGNYGV PSSARDEHGL
     LRYFESPNIQ ASGIVVQDYA LKHSHWTAVE SLAQWCAREG VPAISGVDTR EVVTYLREQG
     SSLARITVGE EYDADEDEAY IDPEAINLVR RVSTKAPFHV SSSLGDMHVA LIDCGVKENI
     LRSLVSRGAS VTCFPFDYPI HKVAHHFDGV FISNGPGDPT HCTSTVYNLR KLFETSQLPV
     MGICMGHQLI ALAAGAKTIK LKYGNRAHNI PALDLTTGKC HITSQNHGYA VDPTTLTSEW
     KEYFTNLNDQ SNEGLIHASR PIFSAQFHPE AKGGPMDSSY LFDKYIQNVQ RYKDHQSSFS
     EKSNKPSPLL VDLLSKERVG VHPAQPDFEM HVPGRVEQVD VGGPVAPPYQ PITAAA
//