ID D0R3X9_LACJF Unreviewed; 362 AA. AC D0R3X9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 04-MAR-2015, entry version 35. 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 RT competitive exclusion agent against pathogens in poultry."; RL J. Bacteriol. 191:7142-7143(2009). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|HAMAP-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 CC the 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 -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-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; FN298497; CAX66792.1; -; Genomic_DNA. DR RefSeq; WP_012846092.1; NC_013504.1. DR RefSeq; YP_003293059.1; NC_013504.1. DR ProteinModelPortal; D0R3X9; -. DR STRING; 633699.FI9785_922; -. DR MEROPS; C26.963; -. DR EnsemblBacteria; CAX66792; CAX66792; FI9785_922. DR GeneID; 8571245; -. DR KEGG; ljf:FI9785_922; -. DR PATRIC; 32246435; VBILacJoh137736_0849. DR eggNOG; COG0505; -. DR HOGENOM; HOG000038087; -. DR KO; K01956; -. DR OrthoDB; EOG61ZTH6; -. DR BioCyc; LJOH633699:GJ95-860-MONOMER; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000002627; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0006543; P:glutamine catabolic process; IEA:InterPro. 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; IPR029062; Class_I_gatase-like. 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 Complete proteome {ECO:0000313|Proteomes:UP000002627}; 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 Glutamine amidotransferase type-1. FT {ECO:0000256|HAMAP-Rule:MF_01209}. FT REGION 1 169 CPSase. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 246 246 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 331 331 {ECO:0000256|HAMAP-Rule:MF_01209}. FT ACT_SITE 333 333 {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 //