UniProt: B2A5V8

Database: UniProt
Entry: B2A5V8_NATTJ

LinkDB:  B2A5V8_NATTJ 
Original site:  B2A5V8_NATTJ

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   B2A5V8_NATTJ            Unreviewed;       430 AA.
AC   B2A5V8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
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   OrderedLocusNames=Nther_0455 {ECO:0000313|EMBL:ACB84051.1};
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB84051.1, ECO:0000313|Proteomes:UP000001683};
RN   [1] {ECO:0000313|EMBL:ACB84051.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB84051.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RX   PubMed=21642468; DOI=10.1128/JB.05157-11;
RA   Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA   Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA   Kyrpides N., Wiegel J.;
RT   "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT   Natranaerobius thermophilus JW/NM-WN-LF.";
RL   J. Bacteriol. 193:4023-4024(2011).
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; CP001034; ACB84051.1; -; Genomic_DNA.
DR   RefSeq; WP_012446938.1; NC_010718.1.
DR   AlphaFoldDB; B2A5V8; -.
DR   STRING; 457570.Nther_0455; -.
DR   KEGG; nth:Nther_0455; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_030949_0_1_9; -.
DR   InParanoid; B2A5V8; -.
DR   OrthoDB; 9768878at2; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000001683; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001683}.
FT   DOMAIN          349..429
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   430 AA;  49518 MW;  6B8A36E92E523F18 CRC64;
     MIERYQRPEM KQLWSLENKF KKWLQVEIYS CEAFSELGEV PGEAVDKIKS NAYFDTQRVL
     ELEKETRHDV IAFTRAVSET LGPEKKYVHY GLTSSDVVDT ALSSLIRDAL TLIEQELDRV
     LQILRDQARK YKDYPIIGRT HGVHAEPTTL GLKFALFYDE LSRSRKRLDR AKENISVGKI
     SGAVGTYANV SPYVEEYVCH KLGLQPALTS TQILQRDRHA ELMSTLAILA GTMDKIATEI
     RNLQKTEVRE VEEPFYKGQK GSSAMPHKRN PVNCEKISGL SRVIRSNAQA AFENQPLWHE
     RDISHSSVER LIIPDSTTLS HYLLNLLAKV LENLHVYPDN MEQNLKTTNG LIYSQRVLLN
     LIDKGLSREK AYDLIQELAM KSWEGDENFQ ELLKQDSRVL EILDKEEIDN CFDPTYYTRN
     VDYIFERLGI
//

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