ID   CARA_PORPU              Reviewed;         384 AA.
AC   P51201;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=carA;
OS   Porphyra purpurea.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 1/6.
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: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the carA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; U38804; AAC08087.1; -; Genomic_DNA.
DR   PIR; S73122; S73122.
DR   RefSeq; NP_053811.1; -.
DR   HSSP; P00907; 1JDB.
DR   GeneID; 809825; -.
DR   BRENDA; 6.3.5.5; 279956.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hyd...; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01209; -; 1.
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   Chloroplast; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Plastid; Pyrimidine biosynthesis.
FT   CHAIN         1    384       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112371.
FT   DOMAIN      196    382       Glutamine amidotransferase type-1.
FT   REGION        1    192       CPSase.
FT   ACT_SITE    272    272       Nucleophile (By similarity).
FT   ACT_SITE    355    355       By similarity.
FT   ACT_SITE    357    357       By similarity.
SQ   SEQUENCE   384 AA;  43296 MW;  D0C45C21FB28E56B CRC64;
     MIKKIPAILV LEDGTYYKGW SFQADQSIVT IGEVVFNTGM TGYQEIITDP SYFQQIVTFT
     YPEIGNTGIN SEDIESQTIS IKGLVAKNIC KISSSWRQQE SLVQYLNRYK IPFIFGIDTR
     SLTQYLRRSG TMNGCISNKN LNHAYLQRKI SEVPHMTGLD LIPNVTTNIM YDWDEKSLPS
     WYLADRNREK IYSQLKVIVI DFGVKLNILR RLATLGCQIT VMPASTPTQD ILSCKPDGIL
     LSNGPGDPSA VNYGIKTVKE LLNQNIPIFG ICMGHQILNL ALEAKTFKLK FGHRGINHPS
     GLKQQVEITS QNHGFAVDLQ SVLKLSLQVT HFNLNDITVA GTGHSRSPYF SVQYHPESSP
     GPHDADYLFE YFIEIMKQFR KEAN
//