ID   A0A1W0A9C1_9STRA        Unreviewed;       509 AA.
AC   A0A1W0A9C1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:OQS06771.1};
GN   ORFNames=THRCLA_01202 {ECO:0000313|EMBL:OQS06771.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS06771.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQS06771.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS06771.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQS06771.1}.
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DR   EMBL; JNBS01000308; OQS06771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W0A9C1; -.
DR   STRING; 74557.A0A1W0A9C1; -.
DR   OrthoDB; 35837at2759; -.
DR   Proteomes; UP000243217; 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:UP000243217}.
SQ   SEQUENCE   509 AA;  56268 MW;  E9833446EE3257B3 CRC64;
     MAGPTCLSAD LGAPLPDHVH AVSVSMPKWE HVERYEQGCP DLHAALRSGY PRFVYHTYVK
     ALNARYHEVF GLDTSKTLFV LPTLTVAERC RDFIECTFPK DCVEIKSLCV IDAHAIIVPV
     EAAACFKSFW QHSGELISSR LAHYILDVLQ NRQVGEKIEF KMDLTPAHTA LRERIGSLYT
     TSGSNVNLYP SGMASIFAAF RLVQKLKQST PGKTVLVGFP YLDTLKMMRR TEWSNGDVLF
     FPRGDKNDID AIDALENIHA IFTEFPSNPL LQSTDLPRLA AIAHRHNTVL VVDDTVGSYN
     VNVLSETHGH AADLVASSLT KIFCGTGTVM GGSLIANPAS PLFSTIQSLL ENDSFLFEDD
     VVALLQASED IHARLARINA TAATIAYRLK HHSMVETIYY PKYINTSQYE HYNSKAAESD
     AHGPLLSLVV RGGQTAAKTF YDALTFAKGP SLGTNFTLSC PYTLLAHYDE LDYVESCGVP
     RDLIRISIGL EDVEEVWSCL ERALDKACE
//