ID A0A165E3Z7_EXIGL Unreviewed; 545 AA.
AC A0A165E3Z7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KZV86025.1};
GN ORFNames=EXIGLDRAFT_841047 {ECO:0000313|EMBL:KZV86025.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86025.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV86025.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86025.1,
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; KV426168; KZV86025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165E3Z7; -.
DR STRING; 1314781.A0A165E3Z7; -.
DR InParanoid; A0A165E3Z7; -.
DR OrthoDB; 5486605at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF1; AROMATIC AMINO ACID AMINOTRANSFERASE, HYPOTHETICAL (EUROFUNG); 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transferase {ECO:0000313|EMBL:KZV86025.1}.
FT DOMAIN 118..400
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 60679 MW; 3E9BE00E63A38C5D CRC64;
MSSYNEKARP KANAVELGHH LSELSKKRTT SPLKGMQKLI LPPGTIKMAG GQPDPLYFPF
ASIGGEAMAP DSYALQPTDA KPSKRGWFDW FMGKERTTTI TIPRFPTGPN EMSLADSLQY
GPATGVALLQ TFINDFVERV YAPNYENWTT LVHVGNTDGW SRAVQTLCNP GELILTEEWT
YPSAVANSAP YDVKPVAVGM DSEGMSASAL EDVLANWDET ERGAKRPHVM YTVPVGQNPC
GMTMGIERKK EIYEICVKYD VIIVEDDPYY FLQEGTYIHK TDRAASSSLN KENKDFVRSL
APSYLAVDYQ GRVVRLDTFS KTIAPGSRMG FFTCNPVFAE RLERQGETTV QRPCGFGQAL
IGQLLTKQWG LDAYIRWLHG LQAQYTARRD ALVDGLLDGF EFSLSYGDGA SYLKGLPVYS
CFPKKGGRSF KREKQVGRML SFVAPTSGMF VWVTVHFEGL PPVPEPEDPE DPRDHETRLW
VRLASAGLLI SPGAFFASTA EVRDKKPGEG HYRIAFSMGP LDELTRGMKI FGKEVHAYYE
ESLRA
//