ID A0A1I6BTI5_9BACI Unreviewed; 474 AA.
AC A0A1I6BTI5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
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 ORFNames=SAMN04488577_2348 {ECO:0000313|EMBL:SFQ84232.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ84232.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ84232.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ84232.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOYF01000003; SFQ84232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6BTI5; -.
DR STRING; 1761761.SAMN04488577_2348; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000199578; 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:UP000199578}.
FT DOMAIN 15..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..462
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 474 AA; 52553 MW; 9BE9D6493165B325 CRC64;
MENANVRIEK DFLGSKEVAA NAYYGIQTLR AVENFPITGY RIHGELIRAM AMVKKAAALA
NVEVGRLYEG LGDAIVKAAD EIIEGMWHEY FIVDPIQGGA GTSINMNTNE VIANRGLEIM
GKEKGDYYHL SPNSHVNMAQ STNDAFPTAI HISTLTLLET LLGTMEHMHD IFAEKAKEFD
HIIKMGRTHL QDAVPIRLGQ EFEAYRRVLQ RDIKRIKNTR EHLYEVNMGA TAVGTGLNAN
PKYIKRVVDH LREITGFPLV NAEHLVDATQ NTDAYTEVSA ALKVCMMNMS KIANDLRLMA
SGPRVGFNEI SLPARQPGSS IMPGKVNPVM PELINQVAFQ VIGNDHTICL ASEAGQLELN
VMEPVLVFNL IQSISIMNNA FRVFTDNCLK GIEANQEKLR QDVERSVGII TAVNPHLGYE
PVARIAREAI LTGKSVRELC LKYDVLSEKE LDLILDPYEM TNPGIAGESL LNKD
//
