ID PUR6_CAEEL Reviewed; 423 AA. AC Q10457; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Probable multifunctional protein ADE2; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazole carboxylase; DE EC=4.1.1.21; DE AltName: Full=AIR carboxylase; DE Short=AIRC; GN ORFNames=B0286.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). 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 -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2). 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 3/5. 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 -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-311886, EBI-311886; CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR CC synthetase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR CC carboxylase 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; U39848; AAA80690.1; -; Genomic_DNA. DR PIR; T15309; T15309. DR RefSeq; NP_494771.1; -. DR UniGene; Cel.16061; -. DR DIP; DIP:24510N; -. DR IntAct; Q10457; 1. DR Ensembl; B0286.3; Caenorhabditis elegans. DR GeneID; 173772; -. DR KEGG; cel:B0286.3; -. DR NMPDR; fig|6239.3.peg.5157; -. DR WormBase; WBGene00015116; B0286.3. DR WormPep; B0286.3; CE03863. DR OMA; Q10457; SQCRVVV. DR BRENDA; 4.1.1.21; 672. DR BRENDA; 6.3.2.6; 672. DR NextBio; 881027; -. DR ArrayExpress; Q10457; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase ac...; IEA:EC. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxam...; IEA:EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro. DR GO; GO:0040007; P:growth; IMP:WormBase. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR InterPro; IPR000031; AIR_COase_core. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR001636; SAICAR_synt. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Gene3D; G3DSA:3.40.50.7700; AIR_carboxyl; 1. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR PANTHER; PTHR11609; SAICAR_synt; 1. DR Pfam; PF00731; AIRC; 1. DR Pfam; PF01259; SAICAR_synt; 1. DR ProDom; PD002193; AIR_carboxyl; 1. DR ProDom; PD003043; SAICAR_synt; 1. DR TIGRFAMs; TIGR01162; purE; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Decarboxylase; Ligase; Lyase; KW Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis. FT CHAIN 1 423 Probable multifunctional protein ADE2. FT /FTId=PRO_0000075034. FT REGION 1 263 SAICAR synthetase. FT REGION 264 423 AIR carboxylase. SQ SEQUENCE 423 AA; 46978 MW; 101CD65318C4804A CRC64; MSSLAEIASR PENLELLAEG KTKQIFDIKG EKDYVLIRSK DSLTAFNAVR KNELEGKSRI ASKTTSNVFE YLQLLGLPTH FEKSISETEF VARKCTMIPI EWVARRVATG SFLKRNPGVK EGFRFNDLKL ETFFKDDAND DPQWTDEQIV SNGLMIDHLK IGREEISLMK KMTKLVFRAL EKGWALSNSA LIDMKIEFGV TVEGEILLAD VIDNDSWRVW PENDRRLQLD KQVYRDMKEV TEEGLALVLK NYTKVMDITA TFSKHQQKCH VLVIMGSGSD GVFARKISDE AKKFGLETTL KVSSAHKTTS DTLEVIADFE ESGVPTVVIA VAGRSNGLGP VIAGNSSLPV INCPPPSEST SLDIWSSLRM PNGIGCTTVL DPSEAALAAA KILASHNHIV FGKVLTAQLK NQINIYNANR KLE //