ID T0S3L3_SAPDV Unreviewed; 431 AA.
AC T0S3L3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:EQC39638.1};
GN ORFNames=SDRG_03069 {ECO:0000313|EMBL:EQC39638.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC39638.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC39638.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC39638.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; JH767138; EQC39638.1; -; Genomic_DNA.
DR RefSeq; XP_008606910.1; XM_008608688.1.
DR AlphaFoldDB; T0S3L3; -.
DR STRING; 1156394.T0S3L3; -.
DR EnsemblProtists; EQC39638; EQC39638; SDRG_03069.
DR GeneID; 19943796; -.
DR VEuPathDB; FungiDB:SDRG_03069; -.
DR eggNOG; KOG0053; Eukaryota.
DR InParanoid; T0S3L3; -.
DR OMA; YGGMITF; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EQC39638.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 431 AA; 45841 MW; 95F025D82C4169F0 CRC64;
MSDYTTLQVH AGQEGGEPGS RARAVPIVAS SSFLFDNTDH AGKLFGLEQF GNIYSRIMNP
TNDVFEKRVT ALTGGVASVA VASGQAAQAL TIFTIAQAGD NIVSTSSLYG GTYNQFKVAF
PRLGINVKFA DHAKPDSIES LIDDNTKAIY VETIGNPELE VPDFEAISAI AKAHGIPLIV
DDTFGACGYL AQPIKHGADI VVQSATKWIG GHGTTIGGVV TDAGTFNWGN GKFPLMANPS
PGYHGLNFWE TFGPGGVLGA NACFAIRLRV ESLRDFGACQ SPFGSFLLLQ GLETLSLRVD
RASDNALALA HWLLEHPSVA WVSYPGLESH PSHALAKKYL HRGKFGAVLT FGVVGGLERG
KSFINNVKLS SHLANVGDSK TLVIHPASTT HQQLTTEERA GSGVKEDLVR VSVGIEHIDD
IKADFDQALR V
//