ID CARA_BUCAP Reviewed; 385 AA. AC Q8K9Z6; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 54. 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=BUsg_138; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from HCO(3)(-): step 1/1. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 1/6. 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 (By CC similarity). CC -!- SIMILARITY: Belongs to the carA family. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013218; AAM67706.1; -; Genomic_DNA. DR RefSeq; NP_660495.1; -. DR HSSP; P00907; 1CE8. DR GeneID; 1005955; -. DR GenomeReviews; AE013218_GR; BUsg_138. DR KEGG; bas:BUsg138; -. DR HOGENOM; Q8K9Z6; -. DR OMA; Q8K9Z6; LFDGSNC. DR BioCyc; BAPH198804:BUSG138-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hyd...; IEA:HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01209; -; 1. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR001317; CarbamoylP_synth_GATase. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR011702; GATASE. DR InterPro; IPR017926; GATASE_1. DR InterPro; IPR000991; GATase_class1_C. DR PANTHER; PTHR11405:SF4; CarA_synth_small; 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 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 Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis. FT CHAIN 1 385 Carbamoyl-phosphate synthase small chain. FT /FTId=PRO_0000112262. FT DOMAIN 197 384 Glutamine amidotransferase type-1. FT REGION 1 193 CPSase. FT ACT_SITE 273 273 Nucleophile (By similarity). FT ACT_SITE 357 357 By similarity. FT ACT_SITE 359 359 By similarity. SQ SEQUENCE 385 AA; 42790 MW; 496864F8283BDE54 CRC64; MEDALGQLAV LVLEDGTRFH GRSIGAKGTT VGEVVFNTSI TGYQEIITDP SYSHQIVTLT HPHIGNIGTN CNDEESSKIH IRGLIIRDMS PISSNYRSEK SFSSYLKENN IVAISDIDTR KLTRILRTKG SQNGCIIEDK KENYSVAYQK AKKFLSLQGL DLAKKVSTKF IYNWDKGSFF INKSKSKLEK KKKFLFHIVV YDFGVKRNIL RMLVDRGCYL TVVPAKTDPK IALNLNPDGI FLSNGPGDPR PCDYAIHAIQ CFLKKNIPIF GICLGHQLLA LASGANIIKM KFGHHGGNHP VKEIKTNRVI ITSQNHSFTV DAKNMPNNIA ITHSSLFDGT LQGLCLTDKL AFSFQGHPEA SPGPHDASSL FDHFIKLLNQ VKFSN //