ID   A0A0G2EFD1_9EURO        Unreviewed;       531 AA.
AC   A0A0G2EFD1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   SubName: Full=Putative cystathionine gamma-synthase {ECO:0000313|EMBL:KKY21592.1};
GN   ORFNames=UCRPC4_g03543 {ECO:0000313|EMBL:KKY21592.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY21592.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY21592.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY21592.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY21592.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY21592.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY21592.1}.
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DR   EMBL; LCWF01000083; KKY21592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EFD1; -.
DR   OrthoDB; 35837at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:UP000053317}.
FT   REGION          96..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  59741 MW;  53C2BD3635BF089F CRC64;
     MLFPSRKTSS MCKQFLNTKL PGLDPDAVRI LILQTSQNAG DNVGDNTLQS INVALYCVLY
     PAEHAAVAKQ VWQHTGDGVS SRRAEFFLTA LREGHLQEDE SNSSPKLPSS RSKRGPRRYQ
     KQESLSEHTH DLNGLNASHE APPSDGREFF QFIEERFGRN LNEKLAQKAK VAVRRRIAGT
     LLSNHDLSES VPALEESPFQ RTKGLSEDDV YLFPCGMSSI FNTHQILLAS REQRKSVCFG
     FPYIDTLKVL EKWGPGVLFY GNGTDDDLDH LERRLKNGER FLALFTEFPS NPLLRSPDLQ
     RIRRLADQYD FAIVVDESVG NLINVNVLQY ADVVVSSLTK VFSGDSNVMG GSATLNTQSP
     IYQSIKQAFN TYYEDNYWIE DAVFLERNSR DFISRIERMN YTTEAVIEFL RSSPLIKDVY
     YPNCVPSKKH YDACKNPHGG YGGLFSLTFH AYEHAIAFFD NLHVLKGPSL GTNFTLSCPF
     VIIAHYNELD WAASFGVPRD LVRVAVGLEE KEDLIARFQV ALDAIAKVAS A
//