ID A0A0E8TZR2_MYCTX Unreviewed; 376 AA.
AC A0A0E8TZR2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Carbamoyl phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209,
GN ECO:0000313|EMBL:SGH43080.1};
GN ORFNames=A4S10_01465 {ECO:0000313|EMBL:OMH59300.1}, ERS007665_03077
GN {ECO:0000313|EMBL:CNV47532.1}, ERS027646_02504
GN {ECO:0000313|EMBL:CKS81532.1}, ERS027659_01494
GN {ECO:0000313|EMBL:CKR47045.1}, ERS027661_02826
GN {ECO:0000313|EMBL:CKS26041.1}, ERS053720_00322
GN {ECO:0000313|EMBL:CFH69459.1}, GJE03_07335
GN {ECO:0000313|EMBL:QGK78641.1}, SAMEA2683035_01140
GN {ECO:0000313|EMBL:SGH43080.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:SGH43080.1, ECO:0000313|Proteomes:UP000182946};
RN [1] {ECO:0000313|EMBL:CFH69459.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH69459.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH59300.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59300.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGH43080.1, ECO:0000313|Proteomes:UP000182946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGH43080.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 172
RC {ECO:0000313|EMBL:CKS81532.1, ECO:0000313|Proteomes:UP000048948}, Bir
RC 185 {ECO:0000313|EMBL:CKR47045.1, ECO:0000313|Proteomes:UP000050164},
RC Bir 187 {ECO:0000313|EMBL:CKS26041.1,
RC ECO:0000313|Proteomes:UP000049023}, and D00700688
RC {ECO:0000313|EMBL:CNV47532.1, ECO:0000313|Proteomes:UP000045274};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH59300.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59300.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QGK78641.1, ECO:0000313|Proteomes:UP000388593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00018547 {ECO:0000313|EMBL:QGK78641.1,
RC ECO:0000313|Proteomes:UP000388593};
RA Baines S.L., Goncalves da Silva A., Carter G.P., Jennison A.V.,
RA Rathnayake I.U., Graham R.M.A., Sintchenko V., Wang Q., Rockett R.J.,
RA Timms V.J., Martinez E., Ballard S., Tomita T., Isles N., Horan K.A.,
RA Pitchers W., Stinear T.P., Williamson D.A., Howden B.P., Seemann T.;
RT "Complete microbial genomes for public health in Australia and Southwest
RT Pacific.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small subunit of the glutamine-dependent carbamoyl phosphate
CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl
CC phosphate from the ammonia moiety of glutamine, carbonate, and
CC phosphate donated by ATP, constituting the first step of 2 biosynthetic
CC pathways, one leading to arginine and/or urea and the other to
CC pyrimidine nucleotides. The small subunit (glutamine amidotransferase)
CC binds and cleaves glutamine to supply the large subunit with the
CC substrate ammonia. {ECO:0000256|HAMAP-Rule:MF_01209}.
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:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077,
CC ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|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. Tetramer of
CC heterodimers (alpha,beta)4. {ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC ECO:0000256|HAMAP-Rule:MF_01209}.
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DR EMBL; CFSW01000002; CFH69459.1; -; Genomic_DNA.
DR EMBL; CNFT01000276; CKR47045.1; -; Genomic_DNA.
DR EMBL; CNFU01000647; CKS26041.1; -; Genomic_DNA.
DR EMBL; CNGE01000468; CKS81532.1; -; Genomic_DNA.
DR EMBL; CQPW01000771; CNV47532.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH59300.1; -; Genomic_DNA.
DR EMBL; CP045962; QGK78641.1; -; Genomic_DNA.
DR EMBL; FPTZ01000005; SGH43080.1; -; Genomic_DNA.
DR RefSeq; WP_003407208.1; NZ_WMCK01000013.1.
DR GeneID; 45425362; -.
DR PATRIC; fig|1773.206.peg.1147; -.
DR OMA; CFSVQYH; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000045274; Unassembled WGS sequence.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000048948; Unassembled WGS sequence.
DR Proteomes; UP000049023; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; Chromosome.
DR Proteomes; UP000388593; 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-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 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 NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01209};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}.
FT DOMAIN 2..134
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1..183
FT /note="CPSase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 350
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 352
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 46
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 232
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 234
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 261
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 264
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 302
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 304
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 305
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
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
//
