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Database: UniProt
Entry: A0A1S3TCH0_VIGRR
LinkDB: A0A1S3TCH0_VIGRR
Original site: A0A1S3TCH0_VIGRR 
ID   A0A1S3TCH0_VIGRR        Unreviewed;       358 AA.
AC   A0A1S3TCH0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Probable low-specificity L-threonine aldolase 1 {ECO:0000313|RefSeq:XP_014491464.1, ECO:0000313|RefSeq:XP_022633574.1};
GN   Name=LOC106754043 {ECO:0000313|RefSeq:XP_014491464.1,
GN   ECO:0000313|RefSeq:XP_022633574.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022633574.1};
RN   [1] {ECO:0000313|RefSeq:XP_014491464.1, ECO:0000313|RefSeq:XP_022633574.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014491464.1,
RC   ECO:0000313|RefSeq:XP_022633574.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_014491464.1; XM_014635978.2.
DR   RefSeq; XP_014491467.1; XM_014635981.1.
DR   RefSeq; XP_022633574.1; XM_022777853.1.
DR   STRING; 3916.A0A1S3TCH0; -.
DR   EnsemblPlants; Vradi0083s00870.1; Vradi0083s00870.1; Vradi0083s00870.
DR   GeneID; 106754043; -.
DR   Gramene; Vradi0083s00870.1; Vradi0083s00870.1; Vradi0083s00870.
DR   KEGG; vra:106754043; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000087766; Unplaced.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          7..294
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   COILED          249..276
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   358 AA;  38423 MW;  6EFBADFA18B7EAAC CRC64;
     MVAKIVDLRS DTVTKPTEAM RGAMASAEVD DDVLGRDPSC FRLETEMAKL LGKEAALFVP
     SGTMANLISV LVHCDIRGSE VILGDDSHIH IYENGGIATL GGVHPRTVKN NEDGTMDIDL
     IEAAIRDPKG ELVYPTTRLI CLENTHGNCG GRCLSVEYTD RVGEVAKKHG LKLHIDGARI
     FNASVALGVP VGRLVQAADS VSVCLSKGLG APVGSVIVGS NSFISKARRL RKTLGGGMRQ
     VGILCAAALV ALQENVEKLE SDHKKAKLLA DGLNEIKGLR VKTSSVETNM IYVEIEERLG
     TTASKLCKDL EDYGILLMTV GSSRLRIVFH HQISASDMQY TLSCFQQAVN GVRNENGN
//
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