ID A0A077LNU0_9PSED Unreviewed; 477 AA.
AC A0A077LNU0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PSCI_5418 {ECO:0000313|EMBL:BAP46120.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP46120.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP46120.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP46120.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP46120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077LNU0; -.
DR STRING; 1028989.PSCI_5418; -.
DR KEGG; pses:PSCI_5418; -.
DR HOGENOM; CLU_025566_2_0_6; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000031652; Chromosome.
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:UP000031652}.
FT DOMAIN 35..334
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 353..467
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 477 AA; 53323 MW; 6460A8BA3E024198 CRC64;
MSGDFVYDVR PFQSQTVREH PMQLSSLTAV SPVDGRYGGK TQALRPIFSE YGLIRFRVLV
EVRWLQRLAA HPQITEVPAF SAEANAILDT LADNFLLEHA ERVKEIERTT NHDVKAVEYL
LKEQAAKLPE LNKVSEFIHF ACTSEDINNL SHALMLREGR DTVVLPLMRQ IADAIRELAQ
RFASVPMLSR THGQPASPTT LGKELANVVY RLERQIAQVA AVPLLGKING AVGNYNAHLS
AYPDIDWEAN ARAFIEDELG LEFNPYTTQI EPHDYIAELF DAVARFNTIL IDFDRDIWGY
ISLGYFKQKT VAGEIGSSTM PHKVNPIDFE NSEGNLGIAN ALFQHLASKL PISRWQRDLT
DSTVLRNLGV GFAHSVIAYE ASLKGIGKLE LNEQRIAADL DACWEVLAEP IQTVMRRYNI
ENPYEKLKEL TRGKGISPEA LLTFIDGLDM PGDAKAELKK LTPANYIGNA VAQAKRI
//
