ID A0A0F2SHD7_9FIRM Unreviewed; 467 AA.
AC A0A0F2SHD7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KJS50318.1};
GN ORFNames=VR66_03410 {ECO:0000313|EMBL:KJS50318.1};
OS Peptococcaceae bacterium BRH_c23.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS50318.1, ECO:0000313|Proteomes:UP000033503};
RN [1] {ECO:0000313|EMBL:KJS50318.1, ECO:0000313|Proteomes:UP000033503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS50318.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS50318.1}.
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DR EMBL; LADV01000034; KJS50318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2SHD7; -.
DR PATRIC; fig|1629714.3.peg.1944; -.
DR Proteomes; UP000033503; Unassembled WGS sequence.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017}.
FT DOMAIN 12..338
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 404..457
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 467 AA; 50877 MW; 6DC533BC6B7E91D6 CRC64;
MRQEKDLIGV HEVPDDVYYG IQTLRAVENF PITGYPPHGE LIRALGMVKG AAAEANMYIG
SLNPSIGKAI VQASRELING QFNEQFVVDV IQGGAGTSMN MNANEVIANR AIEILGGKKG
EYFKVHPNTH VNMAQSTNDV FPTAIRIACL NVANDLLESL DSLRQAFADK AQEFDGIIKM
GRTHLQDAVP IRLGQEFAAY AHMLGRDIKR IKEAIRSLEV MNMGATAVGT GLNADPKYIE
KVTEYLRDWT HLPMRLAEDL VDGTQNTDAF MEVSGSLRTL AVNLSKIAND LRLMASGPRT
GLNELNLPPM QPGSSIMPGK VNPVIAEVVN QVAFQVQGND FTIGLACGAG QLELNVMEPV
MVFNLLQSLD ILRNVTRIFR ERCVIGITAN VERCRAMVEN SVGLVTAINP HVGYEVASSV
AKEAILCGRP VCDIVLEKGI LTKEELDVIL NPYEMTKPGI AGAELLR
//
