ID   CARA_BACCL              Reviewed;         364 AA.
AC   P52557;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=pyrAA;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX   PubMed=8206848; DOI=10.1128/jb.176.12.3698-3707.1994;
RA   Ghim S.Y., Neuhard J.;
RT   "The pyrimidine biosynthesis operon of the thermophile Bacillus
RT   caldolyticus includes genes for uracil phosphoribosyltransferase and uracil
RT   permease.";
RL   J. Bacteriol. 176:3698-3707(1994).
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: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
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   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR   EMBL; X73308; CAA51738.1; -; Genomic_DNA.
DR   PIR; I40168; I40168.
DR   AlphaFoldDB; P52557; -.
DR   SMR; P52557; -.
DR   MEROPS; C26.A33; -.
DR   UniPathway; UPA00070; UER00115.
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   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis.
FT   CHAIN           1..364
FT                   /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT                   small chain"
FT                   /id="PRO_0000112248"
FT   DOMAIN          171..358
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          1..167
FT                   /note="CPSase"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  40289 MW;  383A54A839F6631F CRC64;
     MKRQLILEDG SFFVGERFGS LKETTGEVVF NTGMTGYQEI LSDPSYCGQI VTMTYPLIGN
     YGINRDDFEA IRPHVHGFIV KEACVKPSNW RGELTLDEYL KEKGIPGLSG IDTRKLTRLI
     RQYGTLKGMI CGLDVDPVEA AAKLRAMEWP RDQVRRVSTK SAYPSPGRGE RIVLIDFGMK
     HGILRELNKR NCDVIVLPYN ATAEEVLGWH PDGVMLSNGP GDPKDVPEAI EMIRGILGKV
     PLFGICLGHQ LFALACGANT EKMKFGHRGS NHPVKDLRTG KVAITSQNHG YTVTHESLSG
     TRLEVTHIAL NDGTVEGLRH LDVPAFTVQY HPEASPGPED ANPLFDEFLA LIREFNKKGE
     VIHA