ID A0A166VBN7_9HYPO Unreviewed; 354 AA.
AC A0A166VBN7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyridoxal phosphate-dependent transferase, major domain protein {ECO:0000313|EMBL:OAA33484.1};
GN ORFNames=AAL_00949 {ECO:0000313|EMBL:OAA33484.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:OAA33484.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:OAA33484.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:OAA33484.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA33484.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGY01000001; OAA33484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166VBN7; -.
DR STRING; 1081109.A0A166VBN7; -.
DR OrthoDB; 143891at2759; -.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW Transferase {ECO:0000313|EMBL:OAA33484.1}.
FT DOMAIN 40..302
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 354 AA; 38867 MW; 9ACFDF762100CFEC CRC64;
MPDASIAECE EKYSFLDDYS EGAHPQLLEA LVASNHAQAT GYGNDRYSAE ARRSIRAHLG
RDDVGIFFVP SGTSANAISI AACLRPHEAV IAASSGHIVT RETGAVEASG HKIINVPPVN
GKLTPENVIR ALDDNWHFPH MAKPRLVYIS NATEIGTVYS KAELTALKQL CEIKHLLLFM
DGARIGAALT SAKSDLSLPD ILELTDIFWI GGTKNGALLG EAVVVKDEAL AQDFDFYVKQ
HGSLLAKSRV MGVEFAELFR GDLYFDLARR GNAAAAKLSR SIVGAGYDLR AETETNQVFA
VLPLNLVREL QEYFAFYVWE KCGEDWAVVR LLTTWATDVT QLERFNQIVL GWSH
//