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Database: UniProt
Entry: A0A2A2KWC4_9BILA
LinkDB: A0A2A2KWC4_9BILA
Original site: A0A2A2KWC4_9BILA 
ID   A0A2A2KWC4_9BILA        Unreviewed;       418 AA.
AC   A0A2A2KWC4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=WR25_17648 {ECO:0000313|EMBL:PAV78240.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV78240.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV78240.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV78240.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:PAV78240.1}.
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DR   EMBL; LIAE01007591; PAV78240.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2KWC4; -.
DR   STRING; 2018661.A0A2A2KWC4; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT   DOMAIN          71..338
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   418 AA;  46452 MW;  F10CF3C5FE5DF960 CRC64;
     MHISRCRFLS SLPSTSSFCS FRSPQRRHFF RSAKCQFTRS LHWKMPAHQE ETLLPETGYS
     TKVDNASQCI DLRSDTVTLP SAEMKKAMVE AILGDDVFGE DPTVNQLEKR CAALFGKEAA
     LFVLSGTMGN LLAVLSHCQR GDELIVGRHN HIHKWEQGNY AQLGGISATT LKVNPDGTMD
     PNDIEDAIRA NDQHMPRTAL VCIENTHNFA GGKALSTDYL KSVRKLADKH KLKVHMDGAR
     IYNAAIALNV DVSEICSYVD SMMMCFSKGL GAPMGSILVG TRQFIDEARK KRKAVGGGWR
     QAGILAACAN LALDRAVETI ERDHRHAKLL AKGINERTPE ALKSSIHADE KDITNMVLVT
     CKDKVTTSQV VAFFQSHSIL FMAFDSSRIR IVLNWGVCEN DLHKILDIYQ TFVDSIKI
//
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