ID A0A165GNQ9_EXIGL Unreviewed; 492 AA.
AC A0A165GNQ9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=PLP-dependent transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_837549 {ECO:0000313|EMBL:KZV90786.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90786.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90786.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90786.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KV426040; KZV90786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GNQ9; -.
DR STRING; 1314781.A0A165GNQ9; -.
DR InParanoid; A0A165GNQ9; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 492 AA; 54825 MW; DF35E428CC5746BD CRC64;
MDIEEFRKQG YAAIDRICDY YATLEERPVV SQVEPGYLRK LLPESVPEEG EPMEQIAQSF
QDDILPGITH WQHPSFFAYF PSNATFESML GEMYATCVNN PGFNWTCSPA ATELEGVVMD
WAAKMLGLQE DFLHTSGKGG GVMQTTASDS ALTAVVAARS RYQRAHPDIS LDKLVVYTTT
QTHSLGAKAA LVLGLSIRAL PVEADDQYAL RGEVFKAAVE EDKLKGRHPF ILIATVGTTS
SGAVDRLDEI VDVGKDYPDI WIHVDAAWAG VALACPEFRE QAMLEHINAG AHSFCTNFHK
WGLTHFDAST LWVRNRALLT TALDITPEFL RTKAADTGLV IDYRNWHLAL GRRFRSLKLW
FVLRAYGLSG FQAHIRKGVA QAQLFASLIQ QSPYLQIFTP PSLSLVVFRL RDSDEAANRV
FFGHLADRAD VYLTHTEMNG KFCVRFAVGG VHTEEKHIRH AFEVVEEVAK RTIEERGLGV
SLEAEAEGRT DN
//
