ID A0A1M6Z139_9BACT Unreviewed; 480 AA.
AC A0A1M6Z139; A0A1T4QNM5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN02745108_02352 {ECO:0000313|EMBL:SKA05295.1},
GN SAMN05720469_1518 {ECO:0000313|EMBL:SHL24206.1};
OS Fibrobacter intestinalis.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=28122 {ECO:0000313|EMBL:SHL24206.1, ECO:0000313|Proteomes:UP000184275};
RN [1] {ECO:0000313|Proteomes:UP000184275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWOS {ECO:0000313|Proteomes:UP000184275};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SHL24206.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWOS {ECO:0000313|EMBL:SHL24206.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SKA05295.1, ECO:0000313|Proteomes:UP000190449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43854 {ECO:0000313|EMBL:SKA05295.1,
RC ECO:0000313|Proteomes:UP000190449};
RA Peterson S.W.;
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}.
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DR EMBL; FRAW01000051; SHL24206.1; -; Genomic_DNA.
DR EMBL; FUWU01000051; SKA05295.1; -; Genomic_DNA.
DR RefSeq; WP_073306233.1; NZ_JAQYFD010000181.1.
DR AlphaFoldDB; A0A1M6Z139; -.
DR STRING; 28122.SAMN02745108_02352; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000184275; Unassembled WGS sequence.
DR Proteomes; UP000190449; 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; cd03302; Adenylsuccinate_lyase_2; 1.
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:SHL24206.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172}.
FT DOMAIN 369..456
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 480 AA; 54964 MW; 9767B58D4611854F CRC64;
MRDQFESPLI KRYSSKEMSY IFSPQYKFQT WRKLWIFLAE SEMELGLPIT QEQVDELKAH
ATDINFDVAE AEEKRRRHDV MSHVYAYGVQ CPKAKGIIHL GATSAFVGDN TDLIQMQQAM
ILVRKRLCRV MDKLSKFAME YKDMPQLGAT HFQAAQLTTV GKRACLWLQD MLIDLEELNF
LIEVLPFRGV KGTTGTQASF MDLFNGDEEK IMELDRRVTA KAGFKRVLTI TGQTYTRKWD
NRVNQTLCSI AQSLHKFATD MRLMQGNKEV EEPFEKTQIG SSAMAYKRNP MRSERICSLA
RFVMAQVNST AFTQATQWFE RTLDDSANKR LAIPEAFLAM DAMLIIAENV TNGLVVYPKV
IEKRIMAELP FMATENIIME GVKNGGDRQE LHEEIRVMSM EAGKVVKEQG KDNDLLERVL
KNEKFQKLGI TEEKLKEILD LKKFVGRAPG QVKKFVSEEV RPAIDAVPNW DNLDAGELKV
//
