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Database: UniProt
Entry: A0A135LIX5_PENPA
LinkDB: A0A135LIX5_PENPA
Original site: A0A135LIX5_PENPA 
ID   A0A135LIX5_PENPA        Unreviewed;       567 AA.
AC   A0A135LIX5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Pyridoxal phosphate-dependent transferase, major region, subdomain 2 {ECO:0000313|EMBL:KXG48860.1};
GN   ORFNames=PGRI_027300 {ECO:0000313|EMBL:KXG48860.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG48860.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG48860.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG48860.1,
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|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:KXG48860.1}.
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DR   EMBL; LHQR01000065; KXG48860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LIX5; -.
DR   STRING; 5078.A0A135LIX5; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000070168};
KW   Transferase {ECO:0000313|EMBL:KXG48860.1}.
FT   REGION          35..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         325
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   567 AA;  61544 MW;  95C904274274A746 CRC64;
     MSGIAQPSRA DEVQSLLKAV EDLLIPFIRS ADNDPLVSST QKNGTNGTNG TNGHTGLAGT
     SLVDYKKPEE LRDILQLEIP EKGTKQEGLI EVLQKVLKYS VNTWHQGFLD KLYASTNAPG
     VAAELILATL NTNVHVYQVS PALTVIEKYT GQRLANLFGL NGPRAGGISV QGGSASNTTS
     IVIARNNLYP STKADGNGEY KFVLFTSAHG HYSVEKAAQM LGFGSSAVWP VPIDKVGRMI
     PAELEKLVQK AQSEGRTPFY VNATAGTTVM GSFDPFNEIA AICQKYNLWF HIDGSWGGSF
     IFSQRQKHKL AGAEKANSIA INPHKMLGVP VTCSYLLASD MRQFHKANTL PAGYLFHNED
     EPATNGAAEN APELELDSPE VWDLADLTLQ CGRRADSLKL FLGWTYYGNE GYQQQIDSAC
     DIAAHLANTI DQHPDFVLIS ENPPPCLQVC FYYAPGKKFV YPRGLVSNET QRAKNNSKVT
     EQVTHAIVPK GFMVDFAPPS GDEDAAGNGK FFRCVVNVQT TKETVDSLVR AIEEVGPGIV
     ESLKASTSAI PHKRLGERGH GPVVHRV
//
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