ID A0A0G3I3U4_LIBAF Unreviewed; 434 AA.
AC A0A0G3I3U4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
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=G293_04645 {ECO:0000313|EMBL:AKK20544.1};
OS Candidatus Liberibacter africanus PTSAPSY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1277257 {ECO:0000313|EMBL:AKK20544.1, ECO:0000313|Proteomes:UP000035503};
RN [1] {ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|Proteomes:UP000035503};
RA Lin H., Pietersen G., Sahota P., Lou B., Han S., Read D.A., Civerolo E.L.,
RA Gupta G.;
RT "Complete genome sequence of 'Candidatus Liberibacter africanus, bacterium
RT associated with citrus huanglongbing'.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK20544.1, ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|EMBL:AKK20544.1,
RC ECO:0000313|Proteomes:UP000035503};
RX PubMed=26184931;
RA Lin H., Pietersen G., Han C., Read D.A., Lou B., Gupta G., Civerolo E.L.;
RT "Complete Genome Sequence of 'Candidatus Liberibacter africanus,' a
RT Bacterium Associated with Citrus Huanglongbing.";
RL Genome Announc. 3:e00733-15(2015).
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}.
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DR EMBL; CP004021; AKK20544.1; -; Genomic_DNA.
DR RefSeq; WP_047264506.1; NZ_CP004021.1.
DR AlphaFoldDB; A0A0G3I3U4; -.
DR SMR; A0A0G3I3U4; -.
DR STRING; 1277257.G293_04645; -.
DR KEGG; lau:G293_04645; -.
DR PATRIC; fig|1277257.4.peg.1006; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000035503; 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; cd01360; Adenylsuccinate_lyase_1; 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; IPR019468; AdenyloSucc_lyase_C.
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 NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:AKK20544.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU361172}.
FT DOMAIN 352..432
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 434 AA; 49652 MW; B1F881A4C7D80C8B CRC64;
MISRYARTEM TALWSPETKF RIWFEIEAHA CDALAELGII PKEAAKNIWE KGKNVVFNVD
RIIEFETIIK HDVIAFLTHL AEIIGPDARF IHQGMTSSDV LDTCFSIQLM RSTDILLEDM
NQLLDSLKKR AFEHKDTITI GRSHGIHAEP TTFGLKLAMA YAEFSRSRDR LLRAREEIAI
CAISGSVGTF SNIPPYVEQH VAKAMGLKED PISSQIIARD RHAMYFSVLG IIASSIERLA
TEIRHLQRTE ILEVEEFFHP GQKGSSSMPH KRNPILTENL TGLSRLIRSH VIPAMENVAL
WHERDISHSS VERVIGPDAA IHLDFALNRL KNIIEELVVY PDNMKKNLEH LRGLIYSQRI
LLALTQAGVS REEAYQLVQR NAMKVWQNGS IFLDELLADI DIRKVLSEKE ICDKFDHKYH
TKHVDTIFER VFQI
//
