ID   ASPA_HELPJ              Reviewed;         468 AA.
AC   Q9ZLI5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA; OrderedLocusNames=jhp_0594;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06167.1; -; Genomic_DNA.
DR   PIR; H71913; H71913.
DR   RefSeq; WP_001217506.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZLI5; -.
DR   SMR; Q9ZLI5; -.
DR   STRING; 85963.jhp_0594; -.
DR   EnsemblBacteria; AAD06167; AAD06167; jhp_0594.
DR   KEGG; hpj:jhp_0594; -.
DR   eggNOG; COG1027; Bacteria.
DR   OMA; EICENYV; -.
DR   Proteomes; UP000000804; Chromosome.
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..468
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161343"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51937 MW;  B7C6200CBA19442C CRC64;
     MRIEHDFIGQ MEISDEVYYG IQTLRASENF FITNDKLCSY PVFIKSFAQV KKAAALANAQ
     LGLIDEKLKI AICHACDLLV DGKYHDQFIV DMIQGGAGTS TNMNMNEVIA NLALEYMGHQ
     KGEYQFCHPN DHVNRSQSTN DAYPSALKIA IYERLSNLVA PMKALRDAFA QKAKEFAHVI
     KMGRTQLQDA VPMTLGQEFE TYALMVDRDI EQVLDARNWV RELNLGGTVI GTGINSHPDY
     RSLIEKKIQE VTGRPFVMAN NLIEATQSTG AYVQVSGVLK RIAVKLSKVC NDLRLLSSGP
     RAGLNEINLP KMQPGSSIMP GKVNPVIPEV VNQVCFAVIG NDLSVALAAE GGQLQLNVFE
     PVIAYKLFHS FVILGRAIET LTTKCVEGIT ANEKICHDYV FNSIGIVTAL NPHIGYEKSA
     MIAKEALKSD RSIYDIALEK KILTKEQLDD IFKPENMLSP HAFKKHKD