ID A0A0K9G8Y6_9BACI Unreviewed; 474 AA.
AC A0A0K9G8Y6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:KMY42702.1};
GN ORFNames=AC625_23860 {ECO:0000313|EMBL:KMY42702.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY42702.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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}.
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:KMY42702.1}.
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DR EMBL; LFZW01000002; KMY42702.1; -; Genomic_DNA.
DR RefSeq; WP_049683923.1; NZ_LFZW01000002.1.
DR AlphaFoldDB; A0A0K9G8Y6; -.
DR STRING; 1679170.AC625_23860; -.
DR PATRIC; fig|1679170.3.peg.5347; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000037146; 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017};
KW Reference proteome {ECO:0000313|Proteomes:UP000037146}.
FT DOMAIN 14..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..462
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 474 AA; 52360 MW; 733431317BE0724E CRC64;
MLKEKWRIEK DFLGEKRVPS DVYYGIQTIR AAENFPITGY RINEELIKAV AMVKKAAAIA
NMNNQRLDAR LGQAIVQAAD EIIEGRWLSH FIVDPIQGGA GTSLNMNANE VIANRALELL
GYEKSSYHHL SPNTHVNMSQ STNDVFPTAI HISTLKCLGK LLETMYDMNR VIRGKAQQFD
HVIKMGRTHL QDAVPIRLRQ EFEAYSCVLE RDIKRIHQAC QPLYEINMGA TAVGTGLNAD
PVYIEKVVRI LADISGLPLE RAKHLIDATQ NTDSYTEVSA TLKICMINMS KIANDLRLMA
SGPSTGLAEI SLPARQPGSS IMPGKVNPVM PEMINQVAFQ VIGNDHTICA ASEAGQFELN
VMEPVLVFNL LQSISIMKNA FRSFTDYCLA GIEANEAHLK EYVEKSVGVL TAVNPHIGYE
TAARIARKAI LTGKSVRELC IQEGVLSKEE LDLILNPYEM TEPGIAGVAL LDSK
//
