ASPA_HELPY
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 03-AUG-2022, entry version 115.
DE RecName: Full=Aspartate ammonia-lyase;
DE Short=Aspartase;
DE EC=4.3.1.1;
GN Name=aspA; OrderedLocusNames=HP_0649;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC 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 -!- 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; AE000511; AAD07709.1; -; Genomic_DNA.
DR PIR; A64601; A64601.
DR RefSeq; NP_207443.1; NC_000915.1.
DR RefSeq; WP_001217520.1; NC_018939.1.
DR AlphaFoldDB; P56149; -.
DR SMR; P56149; -.
DR DIP; DIP-3567N; -.
DR IntAct; P56149; 2.
DR MINT; P56149; -.
DR STRING; 85962.C694_03355; -.
DR PaxDb; P56149; -.
DR EnsemblBacteria; AAD07709; AAD07709; HP_0649.
DR KEGG; hpy:HP_0649; -.
DR PATRIC; fig|85962.47.peg.699; -.
DR eggNOG; COG1027; Bacteria.
DR OMA; EICENYV; -.
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; IBA:GO_Central.
DR GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..468
FT /note="Aspartate ammonia-lyase"
FT /id="PRO_0000161342"
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; 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