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Database: UniProt
Entry: R5E2A5_9BURK
LinkDB: R5E2A5_9BURK
Original site: R5E2A5_9BURK 
ID   R5E2A5_9BURK            Unreviewed;       467 AA.
AC   R5E2A5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   ORFNames=BN548_01618 {ECO:0000313|EMBL:CCX86588.1};
OS   Parasutterella excrementihominis CAG:233.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Parasutterella.
OX   NCBI_TaxID=1263099 {ECO:0000313|EMBL:CCX86588.1, ECO:0000313|Proteomes:UP000018034};
RN   [1] {ECO:0000313|EMBL:CCX86588.1, ECO:0000313|Proteomes:UP000018034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:233 {ECO:0000313|Proteomes:UP000018034};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCX86588.1}.
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DR   EMBL; CAXE010000081; CCX86588.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5E2A5; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000018034; Unassembled WGS sequence.
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          27..324
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          343..457
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
SQ   SEQUENCE   467 AA;  52494 MW;  56AC947DB38671C3 CRC64;
     MLTPFYFSMN FIVMELSALT AISPLDGRYG RQTAELRDIF SEFALMRARV TVEVEWLIAL
     SEFNLPELKD LSEEDKLYLR GLVSSFSVAD CQAIKDIEKT TNHDVKAVEY WIKSKMTVNE
     HLAAASEFVH FGCTSEDINN TSHALMLSSG RQLICSHLQM IIDKLKGFAH EWAGVSMLSR
     THGQHASPTT VGKEMANVAA RLEFAVQAIE KVKLLAKMNG AVGNYNAHTI AYPDKDWPAF
     ARNVVENRLH LTFNPYTIQI EPHDYMAELF NAITRANTIL IDLDRDIWGY ISLNYFKQQL
     KEGEVGSSTM PHKVNPIDFE NSEGNLGMAD AFFTFLAQKL PISRWQRDLT DSTVLRNLGV
     AFGYSIVGYT SLERGMNKLR LNEEAIAADL DQSWEVLAEA IQTVMRRYGV PHPYEQLKAL
     TRGKGISPET IHEFVATLDI PEDAKASLQK LTPATYIGLA ETLAKEI
//
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