ID   A0A319EE55_ASPSB        Unreviewed;       601 AA.
AC   A0A319EE55;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:PYI07861.1};
GN   ORFNames=BO78DRAFT_86096 {ECO:0000313|EMBL:PYI07861.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI07861.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI07861.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI07861.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) 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; KZ826339; PYI07861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EE55; -.
DR   STRING; 1448318.A0A319EE55; -.
DR   Proteomes; UP000248423; 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:0019346; P:transsulfuration; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transferase {ECO:0000313|EMBL:PYI07861.1}.
SQ   SEQUENCE   601 AA;  66811 MW;  5783A6A34B4AE4C7 CRC64;
     MSTIELGDSI PSLTPHAVSM SLPTWADNVD YETGEKRVMD KIPTGYPRFF IHNLIEVFAD
     GIVAKYGTPD QKAMLFPSRK AAQRCLSFIK AKAESSIAGD VNIIDLFLDK SKEASEIIVK
     VSPSISAVIF HRELFPIAKQ YWQHSGDGIS SRQAELCHSL FSDGKLVDSA PQPLNQKRGP
     KRYQRGSEYQ TFTKEHKVVS EGGKNSQLPL TNDVAETRES TQFLEERFGR NLDVSFVDNA
     KVAIRRRIAG SLVDEVDLAV EPSPKVTSNS RGVPGLSDDN VYLYPCGMNA IFNTHRMMLE
     GRGQLKSIIF GFPYVDTLKI LQKFGPGCLF YGNGSSEDLD DLETRLKAGE RYLALFCEFP
     GNPMLFCPDL KRIRKLADTY DFGVVVDETI GNSVNVQVLP HADVVVSSLT KIFSGDCNVM
     GGSAILNPEG RYHQPLKNAF DADYEDTYWV EDVMFMERNS RDFVTRIKKI NDNAEAICNV
     LLAHPLVKDV YYPKYTPTKP FYEDCRIPTG GYGGLLSFTF HEKAHAVAFF DRIETAKGPS
     LGTNFTLVSP YVVLAHYWEL DWAAGFGVPA DLLRVSVGVE DMEDLKARFT AALQAAEAVG
     A
//