ID A0A135LLT5_PENPA Unreviewed; 517 AA.
AC A0A135LLT5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE SubName: Full=Pyridoxal phosphate-dependent transferase, major region, subdomain 2 {ECO:0000313|EMBL:KXG49931.1};
GN ORFNames=PGRI_058990 {ECO:0000313|EMBL:KXG49931.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG49931.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG49931.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG49931.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:KXG49931.1}.
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DR EMBL; LHQR01000048; KXG49931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LLT5; -.
DR STRING; 5078.A0A135LLT5; -.
DR OMA; WIYPETI; -.
DR OrthoDB; 35837at2759; -.
DR Proteomes; UP000070168; 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 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Transferase {ECO:0000313|EMBL:KXG49931.1}.
SQ SEQUENCE 517 AA; 57152 MW; EB026E8AAB492A51 CRC64;
MKSMNALAAG EDWLTSQLKT QYPRFFFTED VRELSERILS RLGLSSADGV ACLVLRSLPS
VSRCLKAIKD AGGPSDAVIP VQFSQPESLS CEAFWWDIHA IIYPAQYFGA AFTYWINSGD
GISARHAAFC LTGFDYLQSN SPNPAFCTTG PKTLAPEGEQ IPGLHTSGVV ERDCIKHDIA
TLLQPEDPHQ PPPSPNDVFL YPGGMSAINA VARCVGDMGI NSGVFAFGSW LYTETVKILE
QRWPDITIYK KSGDEELDRL EAYLKSGTHI TALWVDVPSN PMLITPDMPR LRRLANEYDF
LILIDGTVGT FVNVDLLPYA DVLMSSLTKM YSGYANVLAG SAVVNPQSPY YEKLHWHLTA
SYEDTFFPGD IAVLYGNSRD FVHRVQVTNN NAEIVAAKLA AHPAVERVNF PTMTARPQYE
SIRRRDGGYG HLLSVIFHDN ETATRFYDGV DIFKGGSFGT VFTLSTPFAQ LATDADRSRF
AEAGIPSHIV RISIGMEDVD ILLDTLFKAI EVAMRRD
//
