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CARA_MYCLE
ID   CARA_MYCLE              Reviewed;         375 AA.
AC   Q9CCR3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
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=ML0535;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
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DR   EMBL; AL583918; CAC30043.1; -; Genomic_DNA.
DR   PIR; G86975; G86975.
DR   RefSeq; NP_301454.1; NC_002677.1.
DR   RefSeq; WP_010907778.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCR3; -.
DR   SMR; Q9CCR3; -.
DR   STRING; 272631.ML0535; -.
DR   PRIDE; Q9CCR3; -.
DR   EnsemblBacteria; CAC30043; CAC30043; CAC30043.
DR   KEGG; mle:ML0535; -.
DR   PATRIC; fig|272631.5.peg.936; -.
DR   Leproma; ML0535; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_2_1_11; -.
DR   OMA; CFNTGMT; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000806; 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; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000112294"
FT   DOMAIN          184..375
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          1..180
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   375 AA;  40166 MW;  2C091EB563C07B67 CRC64;
     MSKALLVLED GRVFTGMPFG AIGQTLGEAV FSTGMSGYQE TLTDPSYHRQ IVVATAPQIG
     NTGWNDQDGE SRDDRIWVAG YAVRDPSPCA SNWRATGTLE DELVRQRIVG IAGIDTRAVV
     RHLRRYGSMK AGVFSGKAMI EPLNIEALVQ HVRTQQSMLG ADLVGEASTL DAYVVEPKGK
     ERFTVAALDL GIKTNTPRNF ARRGIRSYVL PASATFNQIA DIKPHGLFLS NGPGDPATAD
     HVVALTREVL NAGIPLFGIC FGNQILGRAL GLSTYKMVFG HRGINIPVID HATGRVAVTA
     QNHGFALEGE AGQSFDTPFG SAVVSHTCAN DGVVEGVKLA DGRAFSVQYH PEAAAGPHDA
     EYLFDSFVEL MAAQR
 
 
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