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
