ID ASPA_HELPY Reviewed; 468 AA. AC P56149; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 04-NOV-2026, entry version 133. DE RecName: Full=Aspartate ammonia-lyase {ECO:0000250|UniProtKB:P0AC38}; DE Short=Aspartase {ECO:0000250|UniProtKB:P0AC38}; DE EC=4.3.1.1 {ECO:0000250|UniProtKB:P0AC38}; GN Name=aspA; OrderedLocusNames=HP_0649; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Catalyzes the reversible conversion of L-aspartate to CC fumarate and ammonia. {ECO:0000250|UniProtKB:P0AC38}. 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 Evidence={ECO:0000250|UniProtKB:P0AC38}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AC38}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Aspartase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD07709.1; -; Genomic_DNA. DR PIR; A64601; A64601. DR RefSeq; WP_001217520.1; NC_018939.1. DR AlphaFoldDB; P56149; -. DR SMR; P56149; -. DR DIP; DIP-3567N; -. DR FunCoup; P56149; 101. DR IntAct; P56149; 3. DR STRING; 85962.HP_0649; -. DR PaxDb; 85962-HP_0649; -. DR EnsemblBacteria; AAD07709; AAD07709; HP_0649. DR KEGG; heo:C694_03355; -. DR KEGG; hpy:HP_0649; -. DR PATRIC; fig|85962.47.peg.699; -. DR eggNOG; COG1027; Bacteria. DR InParanoid; P56149; -. DR OMA; AAAQCMF; -. DR OrthoDB; 9802809at2; -. DR PhylomeDB; P56149; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; ISS:UniProtKB. DR GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR CDD; cd01357; Aspartase; 1. DR FunFam; 1.10.40.30:FF:000002; Fumarate hydratase class II; 1. DR FunFam; 1.10.275.10:FF:000001; Fumarate hydratase, mitochondrial; 1. DR FunFam; 1.20.200.10:FF:000001; Fumarate hydratase, mitochondrial; 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; IPR004708; ApsA. DR InterPro; IPR051546; Aspartate_Ammonia-Lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR022761; Fumarate-Lyase-like_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00839; aspA; 1. DR NCBIfam; NF008909; PRK12273.1; 1. DR PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1. DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1. DR Pfam; PF10415; FumaraseC_C; 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 3: Inferred from homology; KW Lyase; Reference proteome. FT CHAIN 1..468 FT /note="Aspartate ammonia-lyase" FT /id="PRO_0000161342" FT REGION 315..324 FT /note="SS loop" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT ACT_SITE 316 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 99 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 138 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 139 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 140 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 185 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 317 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 322 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" SQ SEQUENCE 468 AA; 51981 MW; 60111E869302836A CRC64; MRIEHDFIGQ MEISDEVYYG IQTLRASENF FITNDKLCSY PVFIKSFAQV KKAATLANVQ LGLIDEKLKI AICHACDLLI DGKYHDQFIV DMIQGGAGTS TNMNMNEVIA NLALEYMGHQ KGEYQFCHPN DHVNRSQSTN DAYPSALKIA IYERLSNLVA PMKALRDAFA QKAKEFAHVI KMGRTQLQDA VPMTLGQEFE TYALMVDRDI EQVLDARNWV RELNLGGTAI GTGINSHPDY RSLIEKKIQE VTGRPFVMAN NLIEATQSTG AYVQVSGVLK RIAVKLSKVC NDLRLLSSGP RAGLNEINLP KMQPGSSIMP GKVNPVIPEV VNQVCFAVIG NDLSVALAAE GGQLQLNVFE PVIAYKLFHS FVILGRAIET LTTKCVEGIT ANEKICHDYV FNSIGIVTAL NPHIGYEKSA MIAKEALKSD RSIYDIALEK KILTKEQLDD IFKPENMLSP HAFKKHKD //