ID A0A2A9DQS6_9CORY Unreviewed; 478 AA.
AC A0A2A9DQS6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=ATK06_1836 {ECO:0000313|EMBL:PFG28716.1};
OS Corynebacterium renale.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1724 {ECO:0000313|EMBL:PFG28716.1, ECO:0000313|Proteomes:UP000221653};
RN [1] {ECO:0000313|EMBL:PFG28716.1, ECO:0000313|Proteomes:UP000221653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20688 {ECO:0000313|EMBL:PFG28716.1,
RC ECO:0000313|Proteomes:UP000221653};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG28716.1}.
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DR EMBL; PDJF01000001; PFG28716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9DQS6; -.
DR STRING; 1724.GCA_001044175_00474; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000221653; 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; 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:PFG28716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221653}.
FT DOMAIN 14..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 412..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 478 AA; 51911 MW; 73CDB9D420395EC5 CRC64;
MTDHATRVEE DLLGTLEVPA NSYYGIHTLR AVENFPISST TNNDMPAFIR GMVQVKKAAA
LANGRLRTLP QHKSEAIVWA CDQILEEGRC MDQFPIDAFQ GGAGTSLNMN TNEVVANLAL
EKLGFDKGTY SELNPMDDVN MAQSTNDAYP TGLHLGIYYE MQELKEAFDK LQQAFADKGK
EFADVLKMGR TQLQDAVPMT LGEEFTGFSV NLAEELKNLQ QAADELLEVN MGATAIGTGL
NTPDGYQEEV VKALAEVTGL DIVGSPHLIE ATSDNGPYVH AHAAIKRAAM KLSKICNDLR
LLSSGPTAGL SEINLPPRQA GSSIMPGKVN PVIPEVVNQV CFKVFGNDVT ITYAAEAGQL
QLNVMEPAIS QAIFESLSIL KNAADTLRER CVVGITANKD VCAAYVENSI GIVTYLNPFI
GHHNGDVIAR EAGETGKKVR DLVLEKGLLD EEQLNKVLST ENLTYPKFQG KIYEEGEK
//
