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Database: UniProt
Entry: A0A428QLI9_9HYPO
LinkDB: A0A428QLI9_9HYPO
Original site: A0A428QLI9_9HYPO 
ID   A0A428QLI9_9HYPO        Unreviewed;       550 AA.
AC   A0A428QLI9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEP53_003460 {ECO:0000313|EMBL:RSL66194.1};
OS   Fusarium sp. AF-6.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL66194.1, ECO:0000313|Proteomes:UP000287544};
RN   [1] {ECO:0000313|EMBL:RSL66194.1, ECO:0000313|Proteomes:UP000287544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL66194.1,
RC   ECO:0000313|Proteomes:UP000287544};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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:RSL66194.1}.
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DR   EMBL; NKCJ01000051; RSL66194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428QLI9; -.
DR   STRING; 1325737.A0A428QLI9; -.
DR   Proteomes; UP000287544; 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:UP000287544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   550 AA;  61237 MW;  76BB11E1B4D7A589 CRC64;
     MVILKTQSEF GYAPPPQTPY SVITNIPGWD VAQAVRDGDH GPLKRVFHIY PRFAPTHFSA
     LLGQEIAKCV GQEGKAALVY LNPAVWPYTL RHITLESRGK HRMKSEDVSL RCVDIAGHRV
     YTIFVEPQYM PTMMLTWQNP GLGISIRGAE DLLKGVDTVK EVSIESDVLP TPTWTPEGPA
     HQGIRERIVE LLQRAPLDAD KIKCTPKDVF LYPTGMAAIF HSSNLLMEHR PGTIVVLGII
     FHNTYHHLIE ECPHGWKHFG KVDNDGLSDM EEWLEGEKKA ARPVSYVFVE IPGNPTLETP
     DMYRLKKLSE KYGFVLIVDD TVSGFANIDV LPQSDFLLTS LTKSFSGQSN VMGGSVVLNP
     LSPKYDVLRP LFEASHHNEL FASDAEVLLS NSHDFLERTK ILNCNAFAMA RFLHNAKEVP
     GSPVVNVQYP GLLPSKAEYD AVMRRGTPEL PEPGYGCLLT VEFSDVECAM AFYHRCGFYP
     SPHLGGHVTI MFAYNMVVFG KKVEERDYMR GLGVKEESVR ISAGLEGEGD LIDTLKDALE
     AAIEVKKGSK
//
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