ID A0A3P1WIF5_9ACTN Unreviewed; 494 AA.
AC A0A3P1WIF5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:RRD46399.1};
GN ORFNames=EII42_07090 {ECO:0000313|EMBL:RRD46399.1};
OS Tessaracoccus sp. OH4464_COT-324.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD46399.1, ECO:0000313|Proteomes:UP000274803};
RN [1] {ECO:0000313|EMBL:RRD46399.1, ECO:0000313|Proteomes:UP000274803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD46399.1,
RC ECO:0000313|Proteomes:UP000274803};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD46399.1}.
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DR EMBL; RQYZ01000010; RRD46399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1WIF5; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000274803; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; 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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:RRD46399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000274803}.
FT DOMAIN 11..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 410..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 494 AA; 53794 MW; 94D581379BC9281A CRC64;
MNIRIERDSL GEYEVPADAY WGVHTARAVD NFPISRRPIG IYPDFVVAFA QVKQAAARAN
ADLGELDDER ADLIDQACQE IIEGALHDQF IVGVIQGGAG TSSNMNANEV IANRALELAG
REKGDYAYLH PIDHVNRAQS TNDTYPSAVK LAVAAGIRKL IAELQLLQYS FHLKGREYRD
VLKVGRTQLQ DAVPMTLGQE FHGFASTLGE DVQLLEQTLP SLSELNLGAT AIGTGITAHE
DYAPAVMRHL REITGEHRLR TAHDLIEATS DTGVFMLVSS ALKRNAMKIS KICNDLRLLS
SGPQAGLGEI SLPAKQAGSS IMPGKVNPVI PEAVTQVAYV IAGSDVTVSM ASEGGQLQLN
AFEPVMAHMI LQNVTWLRRA IRTLRINCVD GIVANRDRLR RMVQSSVGVV TALSPTIGYQ
AAADLAKAAL RGEGEIRQLV VERGLLTEQQ VDELLNPQSL SNQGPETQSM PKMTPELIAA
IEQELDRSDR RHDY
//
