ID A0A1V6MP36_9ACTN Unreviewed; 480 AA.
AC A0A1V6MP36;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE Short=ASL {ECO:0000256|RuleBase:RU361172};
DE EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN ORFNames=BM536_018325 {ECO:0000313|EMBL:OQD54067.1};
OS Streptomyces phaeoluteigriseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD54067.1, ECO:0000313|Proteomes:UP000184286};
RN [1] {ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA Herron P.R.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OQD54067.1, ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD54067.1,
RC ECO:0000313|Proteomes:UP000184286};
RA Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA Herron P.R.;
RT "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT DSM41896.";
RL Submitted (FEB-2017) 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|RuleBase:RU361172};
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|RuleBase:RU361172};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2. {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|RuleBase:RU361172}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {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:OQD54067.1}.
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DR EMBL; MPOH02000015; OQD54067.1; -; Genomic_DNA.
DR RefSeq; WP_073494798.1; NZ_MPOH02000015.1.
DR AlphaFoldDB; A0A1V6MP36; -.
DR STRING; 114686.BM536_018325; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000184286; 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 Gene3D; 1.10.275.60; -; 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 InterPro; IPR019468; AdenyloSucc_lyase_C.
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; 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:OQD54067.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172}.
FT DOMAIN 372..458
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 480 AA; 52020 MW; 61BF84C35B118D35 CRC64;
MTSAPAKPRI PNVLAGRYAS AELATLWSPE QKVKLERQLW LAVLRAQKDL GIEVPESAIA
DYERVLDQVD LASIAEREKV TRHDVKARIE EFNDLAGHEQ VHKGMTSRDL TENVEQLQMR
LSLELVRDRT VAVLARLGKL AGEHAELVMA GRSHNVAAQA TTLGKRFATA ADELLVAYGR
VEELLGRYPL RGIKGPVGTA QDMLDLLGGD AAKLAELEQR IATHLGFSQA FTSVGQVYPR
SLDYEVVTSL VQLAAAPSSL ARTIRLMAGH ELVTEGFKPG QVGSSAMPHK MNTRSCERVN
GLMVVLRGYA SMTGELAGDQ WNEGDVSCSV VRRVALPDAF FALDGLLETF LTVLDEFGAF
PAVVARELDR YLPFLATTKV LMGAVRAGVG RELAHEAIKE NAVACALAMR EQGAERNELL
DKLAADGRIP LDRAQLDALM ADKLSFTGAA ADQVAIVVGR IEEIVKQRPE AAGYTPGAIL
//
