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
//