ID   CARA_NEOYE              Reviewed;         384 AA.
AC   Q1XDT6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000255|HAMAP-Rule:MF_01209};
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
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:0000255|HAMAP-Rule:MF_01209}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
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DR   EMBL; AP006715; BAE92325.1; -; Genomic_DNA.
DR   RefSeq; YP_536882.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDT6; -.
DR   SMR; Q1XDT6; -.
DR   GeneID; 3978841; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; Chloroplast;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding; Plastid;
KW   Pyrimidine biosynthesis.
FT   CHAIN           1..384
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000275229"
FT   DOMAIN          196..382
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..192
FT                   /note="CPSase"
FT   ACT_SITE        272
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ   SEQUENCE   384 AA;  43221 MW;  64E8214EC3DB7D39 CRC64;
     MMKRIPAILV LEDGAYYKGW SFQQDKQEIT IGEVVFNTGM TGYQEIITDP SYFHQIVAFT
     YPEIGNTGIN NQDIESHSIS IKGLIAKNIC KISSSWREQQ SLVKYLSSNN IPFIFGIDTR
     SLTQYLRQFG TMNGCISTDN LNHSYLKQKI CEIPSMQGLD LIPHVTTRNV YPWDEKSFPN
     WYLTDNIRVH RVIQLKVIVI DFGVKLNILR RLATLGCQIT VVPAHTPLKD ILAYQPDGIL
     LSNGPGDPSA VHYGIQTVTN LLDYNVPIFG ICMGHQILNL ALKAKTFKLK FGHRGINHPS
     GLNQQVEITS QNHGFAVELT SVFESPVRVT HFNLNDTTIA GTGHNQSPYF SVQYHPESSP
     GPHDADYLFE SFIEIMTKSK NKVS