ID A0A0D7F6V3_RHOPL Unreviewed; 435 AA.
AC A0A0D7F6V3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=OO17_04320 {ECO:0000313|EMBL:KIZ47447.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ47447.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ47447.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ47447.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KIZ47447.1}.
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DR EMBL; JXXE01000078; KIZ47447.1; -; Genomic_DNA.
DR RefSeq; WP_044406112.1; NZ_JXXE01000078.1.
DR AlphaFoldDB; A0A0D7F6V3; -.
DR STRING; 1421013.GCA_000504425_01950; -.
DR PATRIC; fig|1076.23.peg.6454; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000032515; Unassembled WGS sequence.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProt.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro.
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:KIZ47447.1};
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 435 AA; 48757 MW; DCE7DF7220BFF665 CRC64;
MIPRYTRPEM AAIWEPLTRF KIWFEIEAHA ATAQAQLGVI PKSAAETIWA KGKDAAFDVA
RIDEIEREVK HDVIAFLTHL AEFVGPDSRF VHQGMTSSDV LDTCFNVQLT RAADILIADV
DRVLAALKTR AFEHKMTPSI GRSHGIHAEP VTFGLKMAYA YAEFSRARER LVTARKEVAT
CAISGSVGTF AHIDPSVEDY VAKAMGLAVE PVSTQVIPRD RAAMYFATLG VIASSVERLA
TEFRHLQRTE VLEAEEFFSE GQKGSSSMPH KRNPVLTENL TGLSRMVRAY VTPAMENVVL
WHERDISHSS AERMMAPDAT VTLDFILNRL AGVIEKLVVY PDNMTKNLDR LGGLIHSQRL
LTALTQKGCS REESYKLVQR NAMPVWRGEG DFQTLLTNDP DMRKYMSAEE IAEQFDLGYH
LKHVDTIFQR VFGNS
//
