GenomeNet

Database: UniProt
Entry: A0A178ADL2_9PLEO
LinkDB: A0A178ADL2_9PLEO
Original site: A0A178ADL2_9PLEO 
ID   A0A178ADL2_9PLEO        Unreviewed;       508 AA.
AC   A0A178ADL2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:OAK94979.1};
GN   ORFNames=IQ06DRAFT_339952 {ECO:0000313|EMBL:OAK94979.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK94979.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK94979.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK94979.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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; KV441723; OAK94979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ADL2; -.
DR   STRING; 765868.A0A178ADL2; -.
DR   InParanoid; A0A178ADL2; -.
DR   OrthoDB; 9643at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF2; SERINE PALMITOYLTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Transferase {ECO:0000313|EMBL:OAK94979.1}.
FT   DOMAIN          122..492
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   508 AA;  56240 MW;  AA01ACF0B9A114EF CRC64;
     MDLQEVQNAT ARFLNDANTH FQRIPGSAIA VRYIKSSYQN DPVRSAIELF LFLFAVRYLL
     APKYSTQKKV QLTDAEIDEL VDDWTPEPLV AAPTQYEELD NEKRPVIVGP TGPKSKLSNG
     RTVTNLASYN YYNFIANETL KEKAIQTLRT YGVGPCGPPG FYGTQDVHMK TEADVAAHLG
     VPACIIYAQS FSTISSVIPS FSKRGDIIVA DKAVNFAVRK GMQISRSTVR WYEHNDMEDL
     ENVLKKVVKE QAKKPLTRRF IITEGLFENI GDVSNLPKLI ELKLKYKFRL ILDETWSYGV
     LGRTGRGVTE AQNVDAAEVD MIIGSLSGPL CAAGGFCAGN EEVVEHQRIS SASYTYSAAL
     PALLSTTASE TISLLQEQPE ILSALRENIK AMRAQLDPRS DWVKTHSAVD NPMLVLVLKP
     EVIEAKKLSI DDQNQILRDV VDECLANGVL VTRLKAFPLG LGVNPRDAGW QPQPSLKVCV
     TSGLTKKETE KAGTIIRHAI TKIVSRRK
//
DBGET integrated database retrieval system