ID CARA_MARMM Reviewed; 390 AA. AC Q0AMR3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 02-SEP-2026, entry version 105. DE RecName: Full=Carbamoyl phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209}; DE AltName: Full=Carbamoyl phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209}; GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; GN OrderedLocusNames=Mmar10_2132; OS Maricaulis maris (strain MCS10) (Caulobacter maris). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Maricaulales; Maricaulaceae; Maricaulis. OX NCBI_TaxID=394221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., RA Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) 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:0000255|HAMAP-Rule:MF_01209}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl CC phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+); 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:0000255|HAMAP- CC Rule:MF_01209}; CC -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase small chain]: CC Reaction=L-glutamine + H2O = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01209}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP- CC Rule:MF_01209}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000449; ABI66424.1; -; Genomic_DNA. DR RefSeq; WP_011644069.1; NC_008347.1. DR AlphaFoldDB; Q0AMR3; -. DR SMR; Q0AMR3; -. DR STRING; 394221.Mmar10_2132; -. DR KEGG; mmr:Mmar10_2132; -. DR eggNOG; COG0505; Bacteria. DR HOGENOM; CLU_035901_2_2_5; -. DR OrthoDB; 9804328at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000001964; 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:0004359; F:glutaminase activity; IEA:RHEA. 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-UniRule. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:L-glutamine metabolic process; IEA:InterPro. 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; IPR050472; Anth_synth/Amidotransfase. 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 NCBIfam; NF009475; PRK12838.1; 1. DR PANTHER; PTHR43418:SF7; CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN; 1. DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 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; Arginine biosynthesis; ATP-binding; KW Glutamine amidotransferase; Ligase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..390 FT /note="Carbamoyl phosphate synthase small chain" FT /id="PRO_1000138866" FT DOMAIN 202..390 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT REGION 1..198 FT /note="CPSase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT ACT_SITE 279 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT ACT_SITE 363 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT ACT_SITE 365 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 53 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 250 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 252 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 280 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 283 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 321 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 323 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" FT BINDING 324 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209" SQ SEQUENCE 390 AA; 40256 MW; 22C04BB8C4D4C25A CRC64; MTSTPTPTPT GALALADGSV FLGHGTGATG IALGEVCFNT AMTGHQEILA DPSYAGQVVC FTFPHVGNVG ANGEDEEAAS PQARKAAVGM IARAKITPPA SWRADTTFEE WLCTRGIVAL TGIDTRALTR KIREGGMQMC AIAHDAAGNI DIEALKAAAA GAPTMEGREL AADVARTEGG DWTEGNWTLG EGYAVGPEDG PRVVVLDYGV KANILRLLTG AGARVAVLPG KASIDDIKAL NPDGVVVSNG PGDPAETGKY ALPTIKAVLD ANIPTLGICL GHQMLALAIG AKTAKMPQGH HGANHPVKNH ETGQVEIVSM NHGFAVDGTT LPANAAETHV SLFDGSNSGF KLTDKPVWAV QHHPEASPGP QDSFGVFDRF VGELKGRVEA //