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
//