ID A0A1Q8RTJ5_9PEZI Unreviewed; 598 AA.
AC A0A1Q8RTJ5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:OLN87634.1};
GN ORFNames=CCHL11_05748 {ECO:0000313|EMBL:OLN87634.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN87634.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN87634.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN87634.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) 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:OLN87634.1}.
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DR EMBL; MPGH01000089; OLN87634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RTJ5; -.
DR STRING; 708187.A0A1Q8RTJ5; -.
DR OrthoDB; 35837at2759; -.
DR Proteomes; UP000186583; 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:UP000186583};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 180..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 65992 MW; E893C8BAA40EE341 CRC64;
MPQLELGQSI PPDTAHAVSV HLPTWRANVG YEEGESWVVN KMVTGYPRSI VALAEDLAAQ
YARPGQKAML FPTARSARRC LAFIEKNADP SVTSDAAVID FGLHPSTDDL SLLRSLSPTV
SAVVYSPEVF PVAKQYWQHT GDGVSSRRAE FCHGLLKEGL LSPIERPTSP VGKVCRGPRR
YHRPSSIDET KTAAHGQTAK SGLQGTATSE TQESLRFLEE RFGRNLDISL VERARSAIKR
RIAGAMTAAD LEASVSSLPP MAQNSRGQEN LQESDVYLFP CGMNAIFNAH RAMLRARGNL
KSVNFGFPYV DTLKILQKFG PGCLFYGHAS EEDLDDLERR LEAGERYLAL FCEFPCNPLL
SCPNLQRIRG LADKYGFGVV VDETIGNFIN IDVLQYADIV VSSLTKIFSG DCNVMGGSAI
LNPSGQYYEA LKSAWAEDLE DTYWPEDVVF MERNSRDFAS RIERINTNSE ALCDILSSHP
LVKRVYYPKV NPTRDNYDLC KLPGGGYGGL FSVVFHEKAH AIAFFDALDT AKGPSLGTNF
TLTSPYVLLA HYQELEWAAD LGVDPDLIRV SVGLEDTDEL RKVFTHALEA AENRKTTS
//