ID A0A1V9ZG07_9STRA Unreviewed; 353 AA.
AC A0A1V9ZG07;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=L-allo-threonine aldolase {ECO:0000313|EMBL:OQR96760.1};
GN ORFNames=ACHHYP_13646 {ECO:0000313|EMBL:OQR96760.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR96760.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR96760.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR96760.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR96760.1}.
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DR EMBL; JNBR01000131; OQR96760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZG07; -.
DR STRING; 1202772.A0A1V9ZG07; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000243579; 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:UP000243579}.
FT DOMAIN 9..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 353 AA; 37328 MW; 9D99111F7EE5D896 CRC64;
MAGRRLVNLV SDTVTQPCAR MRTAMANAIV GDDVHGTDPT VKKLQVVAAE MLGKERALFV
PSGTMSNLIA VGAHCQRGDE IVLGKKSHIF TYEGAGVSAY LGVGMNTVPT QPNGSLSVAD
VESAIRDDDP HYPRTTLVAV ENTHNTCGGR VVPTEAIRDI ASICASHNLK LHMDGARLAN
ASVYLQAPLS ELVASVDSVS LCLSKGLGAP VGSILAGSEE LIYKAMRLRK SLGGGMRQSG
ILAAAALFAL ENNIQRLAED HANARTLARG LSRIPGIVVD EATVETNMVY FTLDAQAVPN
QVFLARMKEL GVLMGGGYGK QQNQIRAVTH LDVTSDDIET VLRTANTVMS TPA
//
