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Database: UniProt
Entry: A0A0J5P7S2_9PAST
LinkDB: A0A0J5P7S2_9PAST
Original site: A0A0J5P7S2_9PAST 
ID   A0A0J5P7S2_9PAST        Unreviewed;       474 AA.
AC   A0A0J5P7S2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:KMK52443.1};
GN   ORFNames=RO21_00920 {ECO:0000313|EMBL:KMK52443.1};
OS   Muribacter muris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Muribacter.
OX   NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK52443.1, ECO:0000313|Proteomes:UP000036270};
RN   [1] {ECO:0000313|EMBL:KMK52443.1, ECO:0000313|Proteomes:UP000036270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK52443.1,
RC   ECO:0000313|Proteomes:UP000036270};
RA   Christensen H., Nicklas W., Bisgaard M.;
RT   "Reclassification of Actinobacillus muris as Muribacter muris.";
RL   Submitted (DEC-2014) 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:KMK52443.1}.
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DR   EMBL; JWIZ01000003; KMK52443.1; -; Genomic_DNA.
DR   RefSeq; WP_047975919.1; NZ_JWIZ01000003.1.
DR   AlphaFoldDB; A0A0J5P7S2; -.
DR   STRING; 67855.RO21_00920; -.
DR   PATRIC; fig|67855.3.peg.1048; -.
DR   Proteomes; UP000036270; 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:KMK52443.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036270}.
FT   DOMAIN          12..344
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          410..462
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   474 AA;  51577 MW;  75766F1153A21820 CRC64;
     MSNTRLEVDL LGEREVPNEA YWGIHTLRAI ENFNISNNTI SDVPEFVRGM VMVKKATALA
     NGELGAIPKK IAKAIVQACD EILVNGRCMD QFPSDVYQGG AGTSVNMNTN EVVANLALEI
     LGHKKGEYQY LDPMDHVNAS QSTNDAYPTG FRIAVYNSVM QLISKVLYLQ QGFENKAAEF
     AQILKMGRTQ LQDAVPMTLG QEFKAFSVLL DEEVKNLKRT AELLLEVNLG ATAIGTGLNT
     PEGYAPLAVK YLSEVTQLPC VLSENLIEAT SDCGAYVMVH GALKRTAVKL SKVCNDLRLL
     SSGPRAGLNE INLPELQAGS SIMPAKVNPV VPEVVNQVCF KVIGNDTAIT FAAEAGQLQL
     NVMEPVIGQA MFESIDILAN ACVNLRDKCI DGITANKDVC ESYVFNSIGI VTYLNPFIGH
     HNGDIVGKIC ATTGKGVKEV VLERGLLTEE QLDDILSVEN LMNPKYKAKR FEDE
//
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