ID A0A2T0B5I0_9CLOT Unreviewed; 470 AA.
AC A0A2T0B5I0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PRR79140.1};
GN ORFNames=CLLI_09850 {ECO:0000313|EMBL:PRR79140.1};
OS Clostridium liquoris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1289519 {ECO:0000313|EMBL:PRR79140.1, ECO:0000313|Proteomes:UP000239706};
RN [1] {ECO:0000313|EMBL:PRR79140.1, ECO:0000313|Proteomes:UP000239706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100320 {ECO:0000313|EMBL:PRR79140.1,
RC ECO:0000313|Proteomes:UP000239706};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium liquoris DSM 100320.";
RL Submitted (MAR-2018) 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:PRR79140.1}.
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DR EMBL; PVXO01000030; PRR79140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0B5I0; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000239706; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000239706}.
FT DOMAIN 11..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..459
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 51099 MW; 8BA5A34C501100E5 CRC64;
MLYRIESDSI GEKQVPKDAY YGVQTLRAYE NFKITGRKIH PELIKALAQI KKAAAITNME
IELLNRKIGN AIVKACDEII EGKLHDEFIT DAIQGGAGTS MNMNANEVIA NRAIEILGGE
KGDYSIVHPN DHVNMGQSTN DVIPTGGKIA TIRLLEKAIA ELNNLDKALM KKSKEFDHVI
KMGRTQLQDA VPIRLGQEFK AYADVIKRDI VRIKRNMDDL RYVSIGATAI GTGLNADEEY
VKNITPNLCK VSGLDLVQCE DLVDGTQNLD TFAAVSGALK VCAIDLSKIS NDLRLLSSGP
RTGIGEINLP PKQNGSSIMP GKINPVIPEV VSQVAFNVIG NDMAITMAAE GGQLELNAFE
PVLYYNLFES IETLANGVDT FIENCVNGIT ANEKHCKDLV ENSVGIITAL CPHVGYKASA
RIAKTAIKTG ESVRELILKE GLLKDAEMDV IFDAYGMTKP GISGKELLKK
//
