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Database: UniProt
Entry: A0A432VYC8_9GAMM
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ID   A0A432VYC8_9GAMM        Unreviewed;       464 AA.
AC   A0A432VYC8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=CWE06_02190 {ECO:0000313|EMBL:RUO21684.1};
OS   Aliidiomarina haloalkalitolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=859059 {ECO:0000313|EMBL:RUO21684.1, ECO:0000313|Proteomes:UP000288212};
RN   [1] {ECO:0000313|EMBL:RUO21684.1, ECO:0000313|Proteomes:UP000288212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK5 {ECO:0000313|EMBL:RUO21684.1,
RC   ECO:0000313|Proteomes:UP000288212};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO21684.1}.
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DR   EMBL; PIPI01000001; RUO21684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432VYC8; -.
DR   OrthoDB; 9768878at2; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000288212; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288212}.
FT   DOMAIN          16..314
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          333..447
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
SQ   SEQUENCE   464 AA;  51932 MW;  0D18200835DB176C CRC64;
     MQLTLSELTA ISPVDGRYGS KTADLRQHVS EFGLIYQRVL VEIRWLQKLA TIADIVEVPE
     LSSSANAALE AIITNFSEAD AARVKEIERT TNHDVKAVEY FLKEKVADHA ELAAVSEFIH
     FACTSEDINN LSHALMLTAA HEQVVKPYLQ QILSALVSHA QSYQSIPMMA RTHGQPATPT
     TMGKEFANVA VRLDRQISAL NQVQFLGKIN GAVGNYNAHL AAYPQVDWHQ VAEEFVTSLG
     LTWNPYTTQI EPHDYIAEWF DALCRINTIL IDLDRDMWGY IALNHFKQKT IEGEVGSSTM
     PHKVNPIDFE NSEGNLGIAN AVLGHLAAKL PISRWQRDLT DSTVLRNLGV GLGYAVIAYQ
     ATLKGLSKLE VNEANLRNEL DQNWELLAEP VQTVMRRYGI EKPYEKLKEL TRGKRVTAED
     LARFIDNLEL TETVKAELKQ LTPANYIGRA EAFVAELPQH LKHL
//
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