ID A0A3P0X3U9_9BACT Unreviewed; 364 AA.
AC A0A3P0X3U9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RRA47339.1};
GN ORFNames=D1Y84_02525 {ECO:0000313|EMBL:RRA47339.1};
OS Acidipila sp. EB88.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA47339.1, ECO:0000313|Proteomes:UP000279598};
RN [1] {ECO:0000313|EMBL:RRA47339.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA47339.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Pold G., Deangelis K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRA47339.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA47339.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Horta L.;
RT "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RRA47339.1}.
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DR EMBL; QWEV01000005; RRA47339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P0X3U9; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000279598; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:RRA47339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000279598};
KW Transferase {ECO:0000313|EMBL:RRA47339.1}.
FT DOMAIN 25..306
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 364 AA; 39094 MW; 2BF14E9E51FDDF91 CRC64;
MALETDILTP ASPSFAHSNP VTTIDLRSDT VTRPTARMRA VMAEAEVGDD VYGEDPTVNA
LEARAAEVFG REAGLFVPTG TMGNQIAIRL HTERGQEVLC EARAHLIDWE MAMVADFNGC
QLRTAYAEDG VFRWEHIKAL IAPKIYYRQQ PGLISLENTH NMAGGIVTPL PVFEEIWEGA
REAGLPVHLD GARIFHAATH LGIGVQELTS GFDSVMFCLS KGLCAPVGSM LVGSGEFIAR
ARSVRKALGG GMRQAGILAA AGLIALDEMP ARLHEDHSNA RILAERLAAL PGVELDLHSV
QSNIVIFYLR GGRDANHVVR ALKDRGVLAG AVGPHAVRFV THHDVDRSAC AHAARIAAEV
LAEA
//
