ID F4C783_SPHS2 Unreviewed; 445 AA. AC F4C783; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058, ECO:0000256|RuleBase:RU361172}; DE Short=ASL {ECO:0000256|RuleBase:RU361172}; DE EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339, ECO:0000256|RuleBase:RU361172}; DE AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717, ECO:0000256|RuleBase:RU361172}; GN OrderedLocusNames=Sph21_3621 {ECO:0000313|EMBL:ADZ80158.1}; OS Sphingobacterium sp. (strain 21). OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ80158.1}; RN [1] {ECO:0000313|EMBL:ADZ80158.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=21 {ECO:0000313|EMBL:ADZ80158.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K., RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.; RT "Complete sequence of Sphingobacterium sp. 21."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N- CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta- CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4- CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) CC and fumarate. {ECO:0000256|ARBA:ARBA00025012}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- CC carboxamido]succinate = 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920, CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00024477}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921; CC Evidence={ECO:0000256|ARBA:ARBA00024477}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate; CC Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, CC ChEBI:CHEBI:456215; EC=4.3.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00024487}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854; CC Evidence={ECO:0000256|ARBA:ARBA00024487}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734, CC ECO:0000256|RuleBase:RU361172}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC {ECO:0000256|ARBA:ARBA00004706, ECO:0000256|RuleBase:RU361172}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000256|ARBA:ARBA00008273, CC ECO:0000256|RuleBase:RU361172}. 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; CP002584; ADZ80158.1; -; Genomic_DNA. DR AlphaFoldDB; F4C783; -. DR STRING; 743722.Sph21_3621; -. DR KEGG; shg:Sph21_3621; -. DR PATRIC; fig|743722.3.peg.3872; -. DR eggNOG; COG0015; Bacteria. DR HOGENOM; CLU_025566_2_0_10; -. DR OrthoDB; 9768878at2; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01598; PurB; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR InterPro; IPR047136; PurB_bact. DR InterPro; IPR013539; PurB_C. DR NCBIfam; TIGR00928; purB; 1. DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1. DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1. DR Pfam; PF08328; ASL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, KW ECO:0000256|RuleBase:RU361172}. FT DOMAIN 14..309 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 328..443 FT /note="Adenylosuccinate lyase PurB C-terminal" FT /evidence="ECO:0000259|Pfam:PF08328" SQ SEQUENCE 445 AA; 49897 MW; 3DCEEBFB8FC46384 CRC64; MSLSPLTAVS PIDGRYHSAT KDLASFFSEA ALIKYRVFVE IEYFIALAET GISQLSALPN KAALRAIYED FSENDAQRIK DLEKTTNHDV KAVEYFIKEK FEAIGLTDSK EFIHFGLTSQ DINNTAIPYS WKEALNKVYY PGIHVLISEI DAMAKQWKAI PMLAKTHGQP ASPTRLGKEL AVFVERLEGQ LNQLKAIPFS AKFGGATGNF NAHHIAYPDI DWVAFGNHLV NDILGLHRSQ KTTQIEHYDN FAAHCDALKR VNNILIDLCR DIWTYISMDY FKQQIIAGQI GSSAMPHKVN PIDFENAEGN LGLANALFEH LAAKLPISRL QRDLTDSTVL RNIGVPFGHT LIAFKSIMRG LKKLILNEDA LRADLEKNWA VVAEAIQTIL RREGYPKPYE ALKDLTRTNE AINQESIAAF INNLNIADPL KEELKAITPW NYTGV //