ID A0A135LF42_PENPA Unreviewed; 398 AA.
AC A0A135LF42;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyridoxal phosphate-dependent transferase, major region, subdomain 2 {ECO:0000313|EMBL:KXG47565.1};
GN ORFNames=PGRI_014350 {ECO:0000313|EMBL:KXG47565.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG47565.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG47565.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG47565.1,
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:KXG47565.1}.
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DR EMBL; LHQR01000065; KXG47565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LF42; -.
DR STRING; 5078.A0A135LF42; -.
DR OMA; YKQDGVG; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
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; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Transferase {ECO:0000313|EMBL:KXG47565.1}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 398 AA; 42426 MW; E5C2A5C1164B12CC CRC64;
MVSTTENGHT AERGFGTLAV HAGSPHDPVT GAVIAPISLS TTYAQTSVGS PVGLYEYTRS
SNPNRDNFEQ AVAALEHAKY ALAFSSGSAA TANVLQSLAA GSHVVSVSDV YGGTHRYFTK
VASAHGVQVT FTPSIELDVE QLIRPETKLI WIETPSNPTL GLVDIRVIAN IAHKHNIQVV
VDNTFMSPYV QNPLDHGADI VVHSVTKYIN GHSDVLMGVA AFNSEALKER LSFLQNAIGA
VPSAFDCWLA HRGLKTLHLR AREATKNATI VAMALEASPH VISVNYPGID SHPDRAIALK
QHRDGMGGGM LSFRIKGGQK AAHDFCKFTK VFTLAESLGG VESLCEVPSS MTHAGIPKEQ
REAAGVFDDL VRMSCGIEDS VDLHADVMQA LSKAAKLA
//
