ID C6X4C5_FLAB3 Unreviewed; 470 AA.
AC C6X4C5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=FIC_00810 {ECO:0000313|EMBL:ACU07263.1};
OS Flavobacteriaceae bacterium (strain 3519-10).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU07263.1, ECO:0000313|Proteomes:UP000001512};
RN [1] {ECO:0000313|EMBL:ACU07263.1, ECO:0000313|Proteomes:UP000001512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU07263.1,
RC ECO:0000313|Proteomes:UP000001512};
RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA Raymond J.A., Christner B.C., Schuster S.C.;
RT "A bacterial ice-binding protein from the Vostok ice core.";
RL Extremophiles 12:713-717(2008).
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; CP001673; ACU07263.1; -; Genomic_DNA.
DR AlphaFoldDB; C6X4C5; -.
DR STRING; 531844.FIC_00810; -.
DR KEGG; fba:FIC_00810; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_10; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000001512; Chromosome.
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; 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 Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:ACU07263.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001512}.
FT DOMAIN 12..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 51763 MW; CD97CEE802CE800C CRC64;
MENFRIESDL LGELKVPIDA YYGVQTQRAV DNFYITGRKM GEYPEFVKAI GYVKLAAVQT
NHALGLIDDK MLDVISEACQ DVIDGKFRDQ FPVDMIQGGA GTSVNMNANE VLANRALEIM
GFEKGDYQHC YPNDHLNLSQ STNDVYPTTV KLAIIMMNHN LVEHLRKLNH SFREKGKEFH
DVIKMGRTQL QDAVPMTLGQ EFEAFAANLD EEIILLNNIS NLFLEINMGG TAIGTGLNAP
EGYPILCAER LAALTGEDFV SAANLVEATP DTGSFLIYSS VLKRTAVKLS KICNDLRLLS
SGPRAGLNEI NLPPMQPGSS IMPGKVNPVI PEVVNQVCFK VIGNDLTVTL AAQAGQLQLN
VMEPVLSECI IESIIFLERA MDTLRTKCID GITANREVCK NMVKNSIGIV TALNPYIGYK
TSTKIAQEAM ETGKSVYDLV LEHKILSQEK LDEILDPKNM LSSHAFVTIV
//
