ID PUR7_CHRSD Reviewed; 236 AA. AC Q1QTP9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; GN Name=purC; OrderedLocusNames=Csal_2813; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 4/5. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. 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; CP000285; ABE60159.1; -; Genomic_DNA. DR RefSeq; YP_574858.1; -. DR GeneID; 4028498; -. DR GenomeReviews; CP000285_GR; Csal_2813. DR KEGG; csa:Csal_2813; -. DR NMPDR; fig|290398.4.peg.2050; -. DR HOGENOM; Q1QTP9; -. DR OMA; Q1QTP9; TAFNAQK. DR BioCyc; CSAL290398:CSAL_2813-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxam...; IEA:HAMAP. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00137; -; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR001636; SAICAR_synt. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR PANTHER; PTHR11609; SAICAR_synt; 1. DR Pfam; PF01259; SAICAR_synt; 1. DR ProDom; PD003043; SAICAR_synt; 1. DR TIGRFAMs; TIGR00081; purC; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; FALSE_NEG. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis. FT CHAIN 1 236 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_1000018687. SQ SEQUENCE 236 AA; 26592 MW; CFB059F46BECE073 CRC64; MEKRDELYAG KAKSVYRTDD PQRLILHFRD DTSAFDGKKK ESLARKGMVN NKFNAFIMEK LQAAGIPTHF EKLIADDECV VKNLEMIPVE CVVRNVAAGG LVRRLGVEEG QTLTPPTFEL FLKDDAHGDP MINESLAETF GWATPEQLAT MKALTFKVND VLKQLFLDGG MLLVDYKLEF GLFDGEVMLG DEFSPDGCRL WDANTREKMD KDRFRQGLGG VIEAYEEVGR RIGISF //