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Database: UniProt
Entry: A0A1Q7LZB5_9CREN
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ID   A0A1Q7LZB5_9CREN        Unreviewed;       445 AA.
AC   A0A1Q7LZB5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058};
DE            EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717};
GN   ORFNames=AUJ07_00770 {ECO:0000313|EMBL:OLD05764.1};
OS   Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC   Archaea; Thermoproteota.
OX   NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD05764.1, ECO:0000313|Proteomes:UP000186658};
RN   [1] {ECO:0000313|EMBL:OLD05764.1, ECO:0000313|Proteomes:UP000186658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC       biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC       succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC       D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC       carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC       ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC       (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC       and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|ARBA:ARBA00008273}.
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:OLD05764.1}.
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DR   EMBL; MNGL01000004; OLD05764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7LZB5; -.
DR   STRING; 1805098.AUJ07_00770; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000186658; 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; 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; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:OLD05764.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          363..443
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
FT   COILED          120..184
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   445 AA;  49883 MW;  E50C43F903313ED3 CRC64;
     MPILPIDSGR YGSLEMRRIF DEENKLQKWL DVEAAISAAQ AYVGDIPKIA AEEIARNANT
     RTVTLERCKE IEKEIHHDLM SMVRALSEAC SGEGRRFVHY GLTSYDIEDT ATGLLFREAF
     LLLGKELEQL ENNLEKMVRK YKNTLAVART HGRHAGVITF GLKLAVWLEE ARRHQERLKQ
     VKSRALVGKV LGLVGNGAGL GKNALKIQER ALAGLGLKPA GLVTQVVQRD IHAEVVCSLA
     LLAASLDKFA TEVRNLQRTE IGEVMEPFDR DKQVGSSALP SKRNPELSER VSSLAKLERG
     LVTPALENIP LWHERDLSNS ASERFIFPMS FILTEEMLRL TNRILSGLEV FPDNMKRNLE
     LSQGLLLAER VVNQLVEAGV PRQDAHERVR RLAMRSFDEK LSFAKVLQED KIVGKRLTSA
     QISDALDYES YLGVTQQLIG MALRK
//
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