ID Q5NIQ1_FRATT Unreviewed; 432 AA.
AC Q5NIQ1; A0A0G2RN49;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
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 Name=purB {ECO:0000313|EMBL:CAG44648.1};
GN OrderedLocusNames=FTT_0015 {ECO:0000313|EMBL:CAG44648.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG44648.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG44648.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2] {ECO:0007829|PDB:4EEI}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH AMP AND SUCCINATE.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Maltseva N., Kim Y., Shatsman S., Anderson W.F., Joachimiak A.;
RT "Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis
RT Complexed with AMP and Succinate.";
RL Submitted (MAR-2012) to the PDB data bank.
RN [3] {ECO:0007829|PDB:5HW2}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FUMARATE.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Chang C., Maltseva N., Kim Y., Shatsman S., Anderson W.F., Joachimiak A.;
RT "Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis
RT Complexed with fumaric acid.";
RL Submitted (JAN-2016) to the PDB data bank.
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}.
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DR EMBL; AJ749949; CAG44648.1; -; Genomic_DNA.
DR RefSeq; WP_003022846.1; NZ_CP010290.1.
DR RefSeq; YP_169091.1; NC_006570.2.
DR PDB; 4EEI; X-ray; 1.92 A; A/B=1-432.
DR PDB; 5HW2; X-ray; 2.05 A; A/B/C/D=1-432.
DR PDBsum; 4EEI; -.
DR PDBsum; 5HW2; -.
DR AlphaFoldDB; Q5NIQ1; -.
DR SMR; Q5NIQ1; -.
DR IntAct; Q5NIQ1; 3.
DR DNASU; 3191235; -.
DR EnsemblBacteria; CAG44648; CAG44648; FTT_0015.
DR KEGG; ftu:FTT_0015; -.
DR PATRIC; fig|177416.18.peg.18; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000001174; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 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; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
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:4EEI, ECO:0007829|PDB:5HW2};
KW Lyase {ECO:0000313|EMBL:CAG44648.1};
KW Nucleotide-binding {ECO:0007829|PDB:4EEI};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT DOMAIN 64..282
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT BINDING 66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 67
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 67
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5HW2"
FT BINDING 67
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 68
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 93
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HW2"
FT BINDING 94
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5HW2"
FT BINDING 94
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HW2"
FT BINDING 94
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 140
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 212
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 301
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 306
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
FT BINDING 310
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:4EEI"
SQ SEQUENCE 432 AA; 49377 MW; 997868B5378D1DF7 CRC64;
MIKRYDVAEI SKIWADENKY AKMLEVELAI LEALEDRMVP KGTAAEIRAR AQIRPERVDE
IEKVTKHDII AFCTSIAEQF TAETGKFFHF GVTSSDIIDS ALSLQIRDSM SYVIKDLEAL
CDSLLTKAEE TKEIITMGRS HGMFAEPMSF GQKFLGAYVE FKRRLKDLKD FQKDGLTVQF
SGAVGNYCIL TTEDEKKAAD ILGLPVEEVS TQVIPRDRIA KLISIHGLIA SAIERLAVEI
RHLHRSDVFE VYEGFSKGQK GSSTMPHKKN PISTENLTGM ARMLRSHVSI ALENCVLWHE
RDISHSSAER FYLPDNFGIM VYALRRMKNT IDNLVVQRDI IEDRVRSTSA YLSSFYLHFL
VANTPFMRED CYKIVQQVAF DLKQGESFSK KLQKVMHDEH NIILDIPEMD FEGIKKTYLK
EIDHVFDRSV KA
//
