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Database: UniProt
Entry: Q8ZPZ6_SALTY
LinkDB: Q8ZPZ6_SALTY
Original site: Q8ZPZ6_SALTY 
ID   Q8ZPZ6_SALTY            Unreviewed;       456 AA.
AC   Q8ZPZ6;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 128.
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   Name=purB {ECO:0000313|EMBL:AAL20161.1};
GN   OrderedLocusNames=STM1232 {ECO:0000313|EMBL:AAL20161.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL20161.1, ECO:0000313|Proteomes:UP000001014};
RN   [1] {ECO:0000313|EMBL:AAL20161.1, ECO:0000313|Proteomes:UP000001014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720
RC   {ECO:0000313|Proteomes:UP000001014};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0007829|PDB:4NSL}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
RA   Banerjee S., Agrawal M.J., Murthy N.M., Balaram H., Savithri H.S.,
RA   N Murthy M.R.;
RT   "Crystallographic and kinetic studies on Adenylosuccinate Lyase from
RT   Salmonella typhimurium.";
RL   Submitted (NOV-2013) to the PDB data bank.
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       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   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC       catalytic and substrate-binding residues to each active site.
CC       {ECO:0000256|ARBA:ARBA00011668}.
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; AE006468; AAL20161.1; -; Genomic_DNA.
DR   RefSeq; NP_460202.1; NC_003197.2.
DR   RefSeq; WP_000423763.1; NC_003197.2.
DR   PDB; 4NSL; X-ray; 3.00 A; A/B/C/D=1-456.
DR   PDBsum; 4NSL; -.
DR   AlphaFoldDB; Q8ZPZ6; -.
DR   SMR; Q8ZPZ6; -.
DR   STRING; 99287.STM1232; -.
DR   PaxDb; 99287-STM1232; -.
DR   GeneID; 1252750; -.
DR   PATRIC; fig|99287.12.peg.1303; -.
DR   HOGENOM; CLU_025566_2_0_6; -.
DR   OMA; TQVNPCD; -.
DR   PhylomeDB; Q8ZPZ6; -.
DR   BioCyc; SENT99287:STM1232-MONOMER; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; cd01598; PurB; 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; 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   InterPro; IPR047136; PurB_bact.
DR   InterPro; IPR013539; PurB_C.
DR   NCBIfam; TIGR00928; purB; 1.
DR   PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   Pfam; PF08328; ASL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4NSL};
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:UP000001014}.
FT   DOMAIN          14..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          331..445
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
SQ   SEQUENCE   456 AA;  51547 MW;  CC0427BC6457B766 CRC64;
     MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH AAIKEVPAFA
     ADANGYLDTL VANFNEEDAA RIKTIERTTN HDVKAVEYFL KEKVAAIPAL HDVSEFIHFA
     CTSEDINNLS HALMLKTARD EVILPYWRQV INAVKDLATQ YRDIPLLSRT HGQPATPSTL
     GKEMANVAYR MERQFRQLNQ VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ
     WNPYTTQIEP HDYIAELFDC IARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH
     KVNPIDFENS EGNLGLSNAV LHHLANKLPV SRWQRDLTDS TVLRNLGVGI GYALIAYQST
     LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVDAEGMK
     QFIDSLALPE AEKTRLKAMT PANYIGRAVT LVDELK
//
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