ID A0A1V6ST15_9EURO Unreviewed; 568 AA.
AC A0A1V6ST15;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c026G02455 {ECO:0000313|EMBL:OQE16900.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE16900.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE16900.1}.
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DR EMBL; MLQL01000026; OQE16900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6ST15; -.
DR STRING; 254877.A0A1V6ST15; -.
DR OrthoDB; 35837at2759; -.
DR Proteomes; UP000191342; 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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT REGION 175..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62480 MW; F5AB342D9A45D745 CRC64;
MLQALGGPVP PNTDHAVSVS LPSWRENVGY EEGEDWVISK MKCGYPRFFV HPIIQKLAQE
IVRRVGDPNL ESATLFPSLK PARICHSFLL SKIPTEKAYK ARIVNFIPSP HTEAGSTVTS
SLSCVIYPKE YASITKQVWQ HSGNGISSRR GEFCLGALED GFLVEDKGFA TAESISQRPC
KGPRRYQSVN GARKGSIGES PPKSNTEDGR DYAQFIEERF GRNLSTSLAN QAKLAVRKRI
AGVLTADAEL PEALETASSE GRVAGISEED VLLYPSGMSA IFNAHQTLLA TRGDLPSICF
GFPYTDTLKI LQKWGPGCVF YGHGSSEDLD DLESRLKAGE RFLGLFTEAP GNPLLKTPDL
KRIRALADQY GFAVVVDETI SNFLNINVLH LADIVVSSLT KIFSGDSNVM GGSAVLNPHA
QYYAALKETY NRDYEDTYWA EDAVFLERNS LKEVHYPKYS PTRPLYDSLR NANGGYGGLF
SVTFHSTAEA IAFFDTIEVL KGPSLGTNFT LSSPYVLLAH YGELDWARSF NVDPDLVRIS
VGLEDVHDLR SRVQRALDAV QSVRQSSA
//
