ID B1PW12_CAMCO Unreviewed; 468 AA.
AC B1PW12;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 13-SEP-2023, entry version 58.
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:ACA61186.1};
OS Campylobacter coli.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195 {ECO:0000313|EMBL:ACA61186.1};
RN [1] {ECO:0000313|EMBL:ACA61186.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=6979 {ECO:0000313|EMBL:ACA61186.1}, and 7474
RC {ECO:0000313|EMBL:ACA61192.1};
RX PubMed=18673073; DOI=10.1089/fpd.2008.0113;
RA Chan K., Elhanafi D., Kathariou S.;
RT "Genomic evidence for interspecies acquisition of chromosomal DNA from
RT Campylobacter jejuni by Campylobacter coli strains of a turkey-associated
RT clonal group (cluster II).";
RL Foodborne Pathog. Dis. 5:387-398(2008).
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; EU497916; ACA61186.1; -; Genomic_DNA.
DR EMBL; EU497917; ACA61192.1; -; Genomic_DNA.
DR AlphaFoldDB; B1PW12; -.
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:ACA61186.1}.
FT DOMAIN 12..342
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 408..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 468 AA; 51792 MW; 7C9C1E03877126DE CRC64;
MGTRKEHDFI GELEISDEVY YGVQTFRAVE NFNISHERLK DFPRFVRALA RVKKAAAMAN
YELGLLDKDI QDAIIKACDK ILEGGYYDQF VVDMIQGGAG TSTNMNANEV IANIALELMG
HKKGEYQYLH PNDHVNLSQS TNDAYPTALH LALHDYLSDL AKAMEHLKKA YERKAEEFKD
VLKMGRTQLQ DAVPMTLGRE FKTFAVMIGE DIQRVLEARK LILEINLGGT AIGTGINSHP
DYPKVVERKI REVTGFEYTV AEDLIEATQD TGAYVQISGV LKRVATKLSK VCNDLRLLSS
GPKCGLNEIN LPKMQPGSSI MPGKVNPVIP EVVNQVCYFV IGADVTVTFA CEGGQLQLNV
FEPVVAYSLF NSVVMLEKAM YTLADKCIDG ITANEKICSD FVYNSVGIVT ALNPYIGYEN
SASIAKEAMS TGKRVADIAL ERGLLSKEQI DEILTPSNML NPHMEAKK
//
