ID E8QG03_HELP7 Unreviewed; 468 AA.
AC E8QG03;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN Name=aspA {ECO:0000313|EMBL:ADU79915.1};
GN OrderedLocusNames=HPIN_03395 {ECO:0000313|EMBL:ADU79915.1};
OS Helicobacter pylori (strain India7).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907238 {ECO:0000313|EMBL:ADU79915.1, ECO:0000313|Proteomes:UP000009059};
RN [1] {ECO:0000313|Proteomes:UP000009059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=India7 {ECO:0000313|Proteomes:UP000009059};
RA Kersulyte D., Mukhopadhyay A., Choudhury A., Nair G.B., Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain India7.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001494,
CC ECO:0000256|RuleBase:RU362017};
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC ECO:0000256|RuleBase:RU362017}.
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DR EMBL; CP002331; ADU79915.1; -; Genomic_DNA.
DR RefSeq; WP_001217495.1; NC_017372.1.
DR AlphaFoldDB; E8QG03; -.
DR KEGG; hpn:HPIN_03395; -.
DR PATRIC; fig|907238.3.peg.680; -.
DR HOGENOM; CLU_021594_4_1_7; -.
DR Proteomes; UP000009059; 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 CDD; cd01357; Aspartase; 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; 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 NCBIfam; TIGR00839; aspA; 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 {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:ADU79915.1}.
FT DOMAIN 11..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..458
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 468 AA; 51925 MW; C5134C254B580EEE CRC64;
MRIEHDFIGQ MEISDEVYYG IQTLRASENF FITNDKLCSY PVFIKSFAQV KKAAALANAQ
LGLIDEKLKI AICHACDLLI DGKYHDQFIV DMVQGGAGTS TNMNMNEVIA NLALEYMGHK
KGEYQFCHPN DHVNRSQSTN DAYPSALKIA IYERLSNLVA PMKALRDAFA QKAKEFSHVI
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
//
