ID   A0A430B219_9ENTE        Unreviewed;       452 AA.
AC   A0A430B219;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 9.
DE   SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:RSU14301.1};
GN   Name=aspA {ECO:0000313|EMBL:RSU14301.1};
GN   ORFNames=CBF29_03090 {ECO:0000313|EMBL:RSU14301.1};
OS   Vagococcus elongatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=180344 {ECO:0000313|EMBL:RSU14301.1, ECO:0000313|Proteomes:UP000287605};
RN   [1] {ECO:0000313|EMBL:RSU14301.1, ECO:0000313|Proteomes:UP000287605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 51432 {ECO:0000313|EMBL:RSU14301.1,
RC   ECO:0000313|Proteomes:UP000287605};
RA   Gulvik C.A.;
RT   "Vagococcus spp. assemblies.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:RSU14301.1}.
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DR   EMBL; NGKA01000003; RSU14301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430B219; -.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000287605; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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   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   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RSU14301.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287605}.
FT   DOMAIN          10..339
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          405..448
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   452 AA;  49132 MW;  9B366BABCEDBA212 CRC64;
     MSRIERDSVG ELAVPKNSYY GVHSLRAKRN FDITGQAFST DFIQSLAQVK KAAALANYRL
     GLLSEEKMTA ITKAATEIIE GQFHDQFIVD PVQGGAGTSS NMNINEMIAN RGIEILGGEK
     GDFSILHPID DVNMGQSTND VFPTAGKLTI LKQIPLLLEQ LEGLSRSFKN KSEEFKDVLK
     LGRTQLSDAV PLTLGQEFHA YYSVTERGIK RLKAAVFEME SINLGGTAIG TGITADPLLS
     ETVLPILNDI TGENLTIAED LIDGTQNIDC YLVISNVLKT IALSLSKVAN DIRLLSSGPR
     AGIGEIIIPS RQNGSSIMPG KINPVIPEVL TQCAFVVAGN DTTISMAVEA GQLELNAFEP
     VIFYKLLESF LLLTNGIHTF TVNCVDGIQA DEVRCQENLE RSTYLATVLS KTIGYTESAD
     IAQESLETGM SIREVARKHG VKDEILDRLS YN
//