ID   CARA_MYCTO              Reviewed;         376 AA.
AC   P9WPK4; L0T6P8; P71811;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
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; OrderedLocusNames=MT1427;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- 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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45692.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70959; D70959.
DR   RefSeq; WP_003407208.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPK4; -.
DR   SMR; P9WPK4; -.
DR   EnsemblBacteria; AAK45692; AAK45692; MT1427.
DR   GeneID; 45425362; -.
DR   KEGG; mtc:MT1427; -.
DR   PATRIC; fig|83331.31.peg.1533; -.
DR   HOGENOM; CLU_035901_2_1_11; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001020; Chromosome.
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;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis.
FT   CHAIN           1..376
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000426936"
FT   DOMAIN          184..376
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          1..181
FT                   /note="CPSase"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  39767 MW;  DF057465F47AE46D CRC64;
     MSKAVLVLED GRVFTGRPFG ATGQALGEAV FSTGMSGYQE TLTDPSYHRQ IVVATAPQIG
     NTGWNGEDSE SRGERIWVAG YAVRDPSPRA SNWRATGTLE DELIRQRIVG IAGIDTRAVV
     RHLRSRGSMK AGVFSDGALA EPADLIARVR AQQSMLGADL AGEVSTAEPY VVEPDGPPGV
     SRFTVAALDL GIKTNTPRNF ARRGIRCHVL PASTTFEQIA ELNPHGVFLS NGPGDPATAD
     HVVALTREVL GAGIPLFGIC FGNQILGRAL GLSTYKMVFG HRGINIPVVD HATGRVAVTA
     QNHGFALQGE AGQSFATPFG PAVVSHTCAN DGVVEGVKLV DGRAFSVQYH PEAAAGPHDA
     EYLFDQFVEL MAGEGR