ID A0A133ZIL2_9CORY Unreviewed; 520 AA.
AC A0A133ZIL2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=HMPREF0307_01022 {ECO:0000313|EMBL:KXB55288.1};
OS Corynebacterium sp. DNF00584.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB55288.1, ECO:0000313|Proteomes:UP000070591};
RN [1] {ECO:0000313|EMBL:KXB55288.1, ECO:0000313|Proteomes:UP000070591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00584 {ECO:0000313|EMBL:KXB55288.1,
RC ECO:0000313|Proteomes:UP000070591};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXB55288.1}.
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DR EMBL; LSCZ01000015; KXB55288.1; -; Genomic_DNA.
DR RefSeq; WP_066488295.1; NZ_KQ959740.1.
DR AlphaFoldDB; A0A133ZIL2; -.
DR GeneID; 79853002; -.
DR PATRIC; fig|1384076.3.peg.1001; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000070591; 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:KXB55288.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070591}.
FT DOMAIN 58..390
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 456..509
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 56587 MW; 54E0A6D391DC9522 CRC64;
MAKTSKKAEE TTAKVEATAA DTAKKADVTT PAPEAAKEEK SAKKSASKKT RTETDLLGDM
EVPADAYYGV HTLRAMENFQ ISYVTINTIP DFIRGMVQVK KATAMANRRL HVLPKKKAEA
IIWACDQILE EGRCMDQFPL DVFQGGAGTS LNMNTNEVVA NLALEHLGEE KGRYDIINPN
DDVNMSQSTN DAYPTGFRLG VYSSLDNLIE RIDALQQAFN DKGNEFQDIL KMGRTQLQDA
VPMTLGDEFK AFAHNLAEEQ SVLRDAQARL LEINLGATAI GTGVNTPAGY RSQVTAALAE
VTGLEIKTAR DLIEATSDCG AYVLVHSVIK RAAMKLSKIC NDLRLLASGP RAGLAEINLP
PRQAGSSIMP GKVNPVIPEV VNQVCFKIFG NDHVVTMAAE AGQLQLNVME PVIGEALFQS
IRIMGNAVDT LREKCVTGIT ANADVCRAYV ENSIGIVTYL NPFIGHHNGD MIAKESLKTG
KGVRDLILEK GLLDEATLDK VLSVENLMHP EFRGQFYIDD
//
