ID E8N531_ANATU Unreviewed; 470 AA.
AC E8N531;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=purB {ECO:0000313|EMBL:BAJ63545.1};
GN OrderedLocusNames=ANT_15170 {ECO:0000313|EMBL:BAJ63545.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63545.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63545.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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; AP012029; BAJ63545.1; -; Genomic_DNA.
DR AlphaFoldDB; E8N531; -.
DR STRING; 926569.ANT_15170; -.
DR KEGG; atm:ANT_15170; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_1_1_0; -.
DR InParanoid; E8N531; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000008922; 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 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:BAJ63545.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922}.
FT DOMAIN 370..455
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 470 AA; 53637 MW; 0DAEACCAE5110228 CRC64;
MTPNYTLYQS PFSWRYASTE MRTLWSEEYK RKLWRKIWVV LARVQSEFGL FSSQVLKELE
EKQNEIDLER SLEIEKTIHH DLMAELQCFS EQCPNAGGYL HIGATSMDIE DNAEAIRLRE
ALEILVKKLD DLLGLTAQKI RLYSEIPSLA FTHLQPAEPT TLGYRIAGFA QELLIHSQKM
RDLKKNLRGK GFKGAVGTAA SYVEILGPDH FDEFEKKMGE ALQLSFFPVS TQTYPRIQDY
QVLVTLAGLG ATLYKFAFDL RLLQSPLYGE WSEPFSVKQV GSSAMPFKRN PIQAEKIDSL
ARLLASLPQV AWENAAHSLL ERTLDDSANR RTILPEAFLI ADELLLTAIR ILKGIKINTN
SIERNLQVYA PFSASERLLM RLVQKGANRQ EMHEVIREHS MQAWLEVTAG KPNPLFTLLQ
SDERIKIFLN AEEISECQNI QSYTGIAARR AQQIAEDIEK YLQASETYSP
//
