ID D0R3X9_LACJF Unreviewed; 362 AA. AC D0R3X9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 26-FEB-2020, entry version 60. 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:CAX66792.1}; GN OrderedLocusNames=FI9785_922 {ECO:0000313|EMBL:CAX66792.1}; OS Lactobacillus johnsonii (strain FI9785). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=633699 {ECO:0000313|EMBL:CAX66792.1, ECO:0000313|Proteomes:UP000002627}; RN [1] {ECO:0000313|EMBL:CAX66792.1, ECO:0000313|Proteomes:UP000002627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FI9785 {ECO:0000313|EMBL:CAX66792.1, RC ECO:0000313|Proteomes:UP000002627}; RX PubMed=19767436; DOI=10.1128/JB.01182-09; RA Wegmann U., Overweg K., Horn N., Goesmann A., Narbad A., Gasson M.J., RA Shearman C.; RT "Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive RT exclusion agent against pathogens in poultry."; RL J. Bacteriol. 191:7142-7143(2009). 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP- CC 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. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP- CC Rule:MF_01209}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}. 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; FN298497; CAX66792.1; -; Genomic_DNA. DR RefSeq; WP_012846092.1; NC_013504.1. DR EnsemblBacteria; CAX66792; CAX66792; FI9785_922. DR KEGG; ljf:FI9785_922; -. DR HOGENOM; CLU_035901_2_1_9; -. DR KO; K01956; -. DR OMA; CFNTGMT; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000002627; 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 {ECO:0000256|HAMAP-Rule:MF_01209}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209, ECO:0000313|EMBL:CAX66792.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}. FT DOMAIN 171..358 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000259|PROSITE:PS51273" FT REGION 1..170 FT /note="CPSase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 246 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 331 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 333 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" SQ SEQUENCE 362 AA; 40282 MW; 48795AF24561CC8E CRC64; MKRYLILEDG SIYEGKGFGA DCESSGEVVF TTGMTGYQEA ITDQSYADQI LVFTNPLIGN YGITLADYES LEPQIKGVIC HQVARHPDNW RMQTTLPKFL KQLNIPGLQG IDTRELVKKL RIHGTLKGRI TDSKENAASI AQELKQRNIT QGVISRVSTK NSYPVPGSKR NIVVIDFGIK HSILRELAER DCNCIVLPYT ATAEEILNLN PDGVLLSNGP GNPEEMLTAA KMVQEVEKHV PLFGICMGHQ VFALANGAST YKMKFGHRGF NHPVREIATG NIGFTSQNHG YAVDPKSIDK ENLMITHVEV NDGTVEGLRH KKYPAFSVQF HPDATPGPHD EDSLFDDFMS MIDQRKEEER HA //