ID A0A1H7W9Q0_9BACI Unreviewed; 474 AA.
AC A0A1H7W9Q0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05192533_101322 {ECO:0000313|EMBL:SEM18064.1};
OS Mesobacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=930146 {ECO:0000313|EMBL:SEM18064.1, ECO:0000313|Proteomes:UP000198553};
RN [1] {ECO:0000313|Proteomes:UP000198553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48,IBRC-M 10115,DSM 25386,CECT 8001
RC {ECO:0000313|Proteomes:UP000198553};
RA Varghese N., Submissions S.;
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; FOBW01000001; SEM18064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7W9Q0; -.
DR STRING; 930146.SAMN05192533_101322; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000198553; 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:UP000198553}.
FT DOMAIN 14..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; 52393 MW; 73F48270827CF14C CRC64;
MSESQIRIER DFLGEREVPI DAYYGIQTLR AVENFPITGY RIHGELIRAL AMVKKAAALA
NMEVGRLYKG LGDVIVQAAD EIIDGEWHDQ FIVDPIQGGA GTSINMNANE VIANRALEIM
GEKKGDYFKL SPNTHVNMAQ STNDAFPTAM HISVLSLLEQ LLVTMKTMHE AFEQKAEEFD
SYIKMGRTHL QDAVPIRLGQ EFKAYSRVIA RDIKRIKNTR MDLYEVNMGA TAVGTGLNAN
PKYIKRVVVH LAEISGQPLV NAEHLVDATQ NTDAYTEVSA ALKVCMMNMS KIANDLRLMA
SGPRVGFNEI SLPPRQPGSS IMPGKVNPVM AEVINQVAFQ VIGNDNTVCL ASEAGQLELN
VMEPVLIFNL IQSISIMNNA FHVFTEHCVK GIEANKEKLQ QDVDRSVGII TAVNPHLGYE
VVARIAREAI LTGKSVRELC LAYDVLTEEE LDLILNPFEM TNPGIAAEEL LNKD
//
