ID A0A1H4FES0_9BACT Unreviewed; 477 AA.
AC A0A1H4FES0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05444145_1109 {ECO:0000313|EMBL:SEA95320.1};
OS Alistipes timonensis JC136.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1033731 {ECO:0000313|EMBL:SEA95320.1, ECO:0000313|Proteomes:UP000183253};
RN [1] {ECO:0000313|EMBL:SEA95320.1, ECO:0000313|Proteomes:UP000183253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25383 {ECO:0000313|EMBL:SEA95320.1,
RC ECO:0000313|Proteomes:UP000183253};
RA de Groot N.N.;
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}.
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DR EMBL; FNRI01000010; SEA95320.1; -; Genomic_DNA.
DR RefSeq; WP_010265966.1; NZ_FNRI01000010.1.
DR AlphaFoldDB; A0A1H4FES0; -.
DR STRING; 1033731.SAMN05444145_1109; -.
DR GeneID; 78311036; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000183253; 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:SEA95320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183253}.
FT DOMAIN 20..351
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 417..470
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 477 AA; 52609 MW; 6B13722417A1E105 CRC64;
MNFTDIKLSG KTRREHDLLG EMEIPAEYYF GVQTMRAVEN FHISRVRLCF FPELIRALAD
VKQGAAMANL ELGLLDPAIA DAIVRACEEL RAGKLREQFV VDMVQGGAGT STNMNANEVI
ANRALELLGH EKGEYQYCHP NNHVNLSQST NDAYPTAVKI ALVRSIEKLV GALRELIAAF
HAKGGEFAHV IKMGRTQLQD AVPMTLGQEF EAYAANLAEE TERLEVNLKL FYEINMGATA
IGTGINADPD YAEVCTRCLR GITGLPLVKA SNMIEATNDT GAFIMNSSAL KRLAVKLSKI
CNDLRLLSSG PRCGLNEINL PPRQPGSSIM PGKVNPVIPE VVNQVAFRVI GNDLTVTIAS
EAGQLELNVM EPIIVHCLFE SIEMLVNAMN TLREKCIVGI TANEEVCRRM VYNSIGLVTA
LNPYLGYETS TMLAKEALET GKGIYDLVLE HKLMSEEELH KVLRPENMVH PRRKIEE
//
