ID A0A2S6FZ68_9CLOT Unreviewed; 462 AA.
AC A0A2S6FZ68;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:PPK48889.1};
GN ORFNames=BD821_1039 {ECO:0000313|EMBL:PPK48889.1};
OS Clostridium algidicarnis DSM 15099.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121295 {ECO:0000313|EMBL:PPK48889.1, ECO:0000313|Proteomes:UP000239863};
RN [1] {ECO:0000313|EMBL:PPK48889.1, ECO:0000313|Proteomes:UP000239863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15099 {ECO:0000313|EMBL:PPK48889.1,
RC ECO:0000313|Proteomes:UP000239863};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) 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:PPK48889.1}.
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DR EMBL; PTIS01000003; PPK48889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6FZ68; -.
DR STRING; 37659.GCA_000703125_01945; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000239863; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:amino acid biosynthetic process; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PPK48889.1}.
FT DOMAIN 12..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 462 AA; 50264 MW; C1571BC2F92BAA56 CRC64;
MDFRIESDSI GSRNVPKEAY YGVQSLRAKE NFKITGLMLN EEFIKGLAET KKAAALVNGS
IGLLDEKIEK ALVKACDEII DGKLHDQFIV DPIQGGAGTS ANMNINEVIS NRAIEILGGE
KGDYKIVHPN DHANMGQSTN DIIPTAGKLA MLRLIDKASN QLNKLYEALV EKSKEFDDVI
KMGRTQMQDA VPIRLGQEFN AYSSLVKRNI SRINNVKEHL KVINMGGTAI GTGINADKRY
FSKIVPKLSE VTKIDLVQAE DLVDATQNLD IFVEVSSVIK TCAVGLSKMS NDLRLMSSGP
RTGFGEINLP SKQNGSSIMP GKVNPVIPEV MNQVAFNIIG NDVTITMAAE AGQLELNAFE
PVIFYNLFQS IETLTSGVDT FTENCIKGIT ANEERCKDLV ENSVGIITAI CPSVGYKVAS
NVAKTSLKTG ESVIDIILRE GILKESELGK ILHPRTMTEP GI
//
