ID A0A1S2LGF1_9BACI Unreviewed; 471 AA.
AC A0A1S2LGF1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=BKP37_18720 {ECO:0000313|EMBL:OIJ10565.1};
OS Anaerobacillus alkalilacustris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ10565.1, ECO:0000313|Proteomes:UP000179524};
RN [1] {ECO:0000313|EMBL:OIJ10565.1, ECO:0000313|Proteomes:UP000179524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ10565.1,
RC ECO:0000313|Proteomes:UP000179524};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
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}.
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:OIJ10565.1}.
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DR EMBL; MLQR01000050; OIJ10565.1; -; Genomic_DNA.
DR RefSeq; WP_071311138.1; NZ_MLQR01000050.1.
DR AlphaFoldDB; A0A1S2LGF1; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000179524; 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}.
FT DOMAIN 12..341
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 407..459
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 471 AA; 51481 MW; 5E5CE0F0FA94F352 CRC64;
MSNVRIERDL MGEKEIPQDA YYGIQTARAI ENFPITGYPP HRELIRAFGF VKKAAAMANR
DVGVLNKKIA DAIVQASDEI IEGKLIEHFV VDSIQGGAGT SFNMNANEVI ANRAIELLGG
KKGDYMTVSP NTHVNMAQST NDTFPTAIHI ACLHLASGLT SSLHELITAL EKKEKEFDQI
IKMGRTHLQD AVPIRLGQEF GAYKRVLSRD LKRIKNSVCH LYEINMGATA VGTGLNAVPE
YITLVAKYLA EHTGMPFKSA EDLVDATQNT DAYTELSSSL KILAINISKI ANDLRLMSSG
PLTGINEINL PPRQAGSSIM PGKVNPVMCE VINQISFQVI GNDHTISLAS EAGQLELNVM
EPVLVFNLLQ SLSILQNGMK VFKEYCIEGI TANRERCLDM VEGSVGIITA INPHVGYEVA
ARIAKEAIQT KRPVREICIE RGILSEEELK VILDPNEMTV PGIAGADLLF E
//
