ID   ASPA_PSEFL              Reviewed;         478 AA.
AC   P07346;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3096982; DOI=10.1093/oxfordjournals.jbchem.a121762;
RA   Takagi J.S., Tokushige M., Shimura Y.;
RT   "Cloning and nucleotide sequence of the aspartase gene of Pseudomonas
RT   fluorescens.";
RL   J. Biochem. 100:697-705(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
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DR   EMBL; D00100; BAA00062.1; -; Genomic_DNA.
DR   EMBL; X04441; CAA28037.1; -; Genomic_DNA.
DR   PIR; A24874; UFPSDF.
DR   AlphaFoldDB; P07346; -.
DR   SMR; P07346; -.
DR   STRING; 690597.JH730931_gene3483; -.
DR   PRIDE; P07346; -.
DR   eggNOG; COG1027; Bacteria.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR004708; ApsA.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_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   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00839; aspA; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..478
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161344"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  51508 MW;  E7903CC4DA7C99C8 CRC64;
     MISVMSSAAS FRTEKDLLGV LEVPAQAYYG IQTLRAVNNF RLSGVPISHY PKLVVGLAMV
     KQAAADANRE LGQLSERKHA AISEACARLI RGDFHEEFVV DMIQGGAGTS TNMNANEVIA
     NIALEAMGHQ KGEYQYLHPN NDVNMAQSTN DAYPTAIRLG LLLGHDALLA SLDSLIQAFA
     AKGAEFSHVL KMGRTQLQDA VPMTLGQEFR AFATTLGEDL ARLKTLAPEL LTEVNLGGTA
     IGTGINADPR YQALAVQRLA TISGQPLVPA ADLIEATSDM GAFVLFSGML KRTAVKLSKI
     CNDLRLLSSG PRTGINEINL PARQPGSSIM PGKVNPVIPE AVNQVAFQVI GNDLALTMAA
     EGGQLQLNVM EPLIAFKIFD SIRLLQRAMD MLREHCIVGI TANEARCREL VEHSIGLVTA
     LNPYIGYENA TRIARIALES GRGVLELVRE EGLLDDAMLD DILRPENMIA PRLVPLKA