ID K2KYD9_HELPX Unreviewed; 468 AA.
AC K2KYD9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:EKE82670.1};
GN ORFNames=OUE_0753 {ECO:0000313|EMBL:EKE82670.1};
OS Helicobacter pylori R030b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145111 {ECO:0000313|EMBL:EKE82670.1, ECO:0000313|Proteomes:UP000006761};
RN [1] {ECO:0000313|EMBL:EKE82670.1, ECO:0000313|Proteomes:UP000006761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R030b {ECO:0000313|EMBL:EKE82670.1,
RC ECO:0000313|Proteomes:UP000006761};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE82670.1}.
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DR EMBL; AMOR01000002; EKE82670.1; -; Genomic_DNA.
DR RefSeq; WP_001217509.1; NZ_AMOR01000002.1.
DR AlphaFoldDB; K2KYD9; -.
DR PATRIC; fig|1145111.4.peg.739; -.
DR Proteomes; UP000006761; Unassembled WGS sequence.
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:EKE82670.1}.
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; 958F0CC00B5C5670 CRC64;
MRIEHDFIGQ MEISDEVYYG IQTLRASENF FITNDKLCSY PVFIKSFAQV KKAAALANAQ
LGLIDEKLKI AICHACDLLV DGKYHDQFIV DMIQGGAGTS TNMNMNEVIA NLALEYMGHQ
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
//
