ID   A0A0D2BX92_9EURO        Unreviewed;       562 AA.
AC   A0A0D2BX92;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV08_05964 {ECO:0000313|EMBL:KIW15914.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15914.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW15914.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15914.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847495; KIW15914.1; -; Genomic_DNA.
DR   RefSeq; XP_016236130.1; XM_016380303.1.
DR   AlphaFoldDB; A0A0D2BX92; -.
DR   STRING; 91928.A0A0D2BX92; -.
DR   GeneID; 27333047; -.
DR   VEuPathDB; FungiDB:PV08_05964; -.
DR   HOGENOM; CLU_011302_3_0_1; -.
DR   OrthoDB; 35837at2759; -.
DR   Proteomes; UP000053328; 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:UP000053328}.
SQ   SEQUENCE   562 AA;  62621 MW;  272E72F70610BD0C CRC64;
     MSAKITTLPG HAIPPAPRHA ITTHLPSWEM LLRFAKDKDP EVINMLESMY PRMILHRDVK
     ELMTKIIEYA GVQNTGQTCR LFPSIQAARD CKVFATSAAR GEGALRDDQL TIHAFTFESH
     ADGAIKNKVN VYAVFFPVAS TSVVHGFWTH SGTGISSRMA EYCLQHIDTL DESERHQNLS
     SEAVGKLTMA ESLAHHQIKD RITTLLKRAP IEPSRTTRLA PHDVYLYSTG MSAIYWVHKC
     LLSKYGSKTV LFGFSFSSTI HVLGAFGPGV EFFGQGDDDD LKLLEEYLSS QKAKDQKVQA
     IWTEVPSNPL LNTPDLKRLR ELADRYGALL IVDDTIGSFC NIDAFGVADI LVTSLTKSFS
     GYADVLASSA VLNPSASRYV ELKALFDETY LNFFFVGDAE TLERNSRNYL ERSAVLNKNA
     EKIVEYLVKE VDDPHSPVKR VYYPTTSKSV EIYQSMMRPE TRDFKPGYGC LFSVEFESLD
     AAVAFYNNLN VHLGPHLGAH LTLAIGYCMG VYPNEQEWVA QYGLLPTQIR VSAGLEETET
     LLEDFRVAVE AAKAAADTRT LN
//