ID   X0BL94_FUSOX            Unreviewed;       562 AA.
AC   X0BL94;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOQG_13047 {ECO:0000313|EMBL:EXK82621.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK82621.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK82621.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK82621.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; JH658411; EXK82621.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0BL94; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_011302_1_0_1; -.
DR   Proteomes; UP000030663; 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:UP000030663};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   562 AA;  63397 MW;  B41216A6B0B6281A CRC64;
     MSETNAGRNW VCPNSLRALP LHEAHIHPPG TPHAVSSSLP TWESVVALAS ADKTVLDRID
     YSYPRFFIGK PIRSLVERVR ERLKFDSDDL VCYIFPSADD ADDYAAQLRK KNAVVHHVRL
     FSPVAANSSN GNDYLAFSAL FVPPDFKVYV MEFWVNFGTG ITTRHAEYCL KHFDELISDS
     PDVKPVTADI PSHDRSSEAW IQRGPRDLED LQAHIAQLAT SKRDDLKPVQ ATDVFIFPNG
     MNAIYNAAEV IAVNNPDSFV VAFGWIYPET IENLRRGTWK DVIPFKLGNE EELDQLASTL
     KTNEQIIAIF CELPSNIKFT SPNLHRIREL ANEYGLIVVC DETVANFVNV DLLPYVDIIT
     TSLTKMFSGA ANVTGGSVIV NPNFGHYEEL HYALRCRYPV VTCFPKDIAV LKQNSINMVE
     RVKKANENTL IVIDRFENHP SVAYVNYPSR PATIQNYERH RRKNGGYGNV FSVVFHNPES
     AQYFYDNLDV CKGPSFGTNF TLAIPFVQLA VYNVREKLEK YDLPKHIIRI SVGLENSRQI
     CSKMEEALAK VVRFEQSLGS QA
//