ID A0A078LYF2_9PSED Unreviewed; 474 AA.
AC A0A078LYF2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BN1079_02203 {ECO:0000313|EMBL:CDZ94876.1};
OS Pseudomonas saudiphocaensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ94876.1, ECO:0000313|Proteomes:UP000053902};
RN [1] {ECO:0000313|EMBL:CDZ94876.1, ECO:0000313|Proteomes:UP000053902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ94876.1,
RC ECO:0000313|Proteomes:UP000053902};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCSF01000001; CDZ94876.1; -; Genomic_DNA.
DR RefSeq; WP_037024273.1; NZ_JADDOO010000001.1.
DR AlphaFoldDB; A0A078LYF2; -.
DR STRING; 1499686.BN1079_02203; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_6; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000053902; 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; 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:CDZ94876.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053902}.
FT DOMAIN 15..347
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..465
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 474 AA; 51082 MW; A57C2B8BBD8EA930 CRC64;
MSSAASFRIE KDLLGTLEVP ADAYYGIQTL RAVNNFRLSG VPLSHYPKLV VALAMVKQAA
ADANRELGHL SDAKHRAISQ ACAQLIRGDY HDQFVVDMIQ GGAGTSTNMN ANEVIANLAL
ESMGHAKGEY HHLHPNNDVN MAQSTNDAYP TAIRLGLLLG HDTLLASLES LVAAFADKGA
EFAHVLKMGR TQLQDAVPMT LGQEFHAFAT TLGEDLEHLR LIAPQLLVEV NLGGTAIGTG
INADPSYQAL AVQRLATISG HPLKPAADLI EATSDMGAFV TFSSMLKRLA VKLSKICNDL
RLLSSGPRTG INEINLPPRQ PGSSIMPGKV NPVIPEAVNQ VAFEVIGNDL SLTIAAEAGQ
LQLNVMEPLI AYKLFDSIRL LQRAMDMLRE HCVSGITANE DRCRQLMESS IGLITALNPY
IGYENATRIA GQALLSGRGV LELVREERLL DDATLDDILR PENMIAPRLV PLQG
//
