ID A0A366S2M8_9HYPO Unreviewed; 454 AA.
AC A0A366S2M8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIESC28_03600 {ECO:0000313|EMBL:RBR23587.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR23587.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR23587.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR23587.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) 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}.
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:RBR23587.1}.
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DR EMBL; QKXC01000073; RBR23587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366S2M8; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000253153; Unassembled WGS sequence.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 429..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 454 AA; 49146 MW; 1292E83B9FE074FA CRC64;
MSEELSKNFE TLQLHAGAEI DPTTRSRGVP IYATTSYVFN DSAQGARLFG LKEFGNIYSR
IMNPTVDVFE KRIAALEGGV AALAASSGQA AQFLAISTLA HAGDNIVSTS NLYGGTYNQF
KVFFPRLGIN TKFVDGDKPE DIAAAIDEKT KAVYVESIGN PKYNIPDLEA ISKAAHEKGV
PVIVDNTFGA GGYFIRPIDH GADIVVHSAT KWIGGHGTTI GGVVVDSGKF DWGKHAARFP
QFHEPSEGYH GLKFYETFGN ITFIIRARVE ILRDLGSTLN PFAAQQLLLG LETLSLRAER
HAQNALALAQ YLEKSPYVSW VSYPGLESHP YHETAKRYLK RGFGGVLSFG VKGGGAGSEV
VDGFKLISNL ANVGDAKTLA IHPWSTTHEQ LSDDEKRRSG VTEDLIRISV GIEHIDDIIA
DFEQSFKAAS DTTTKGEKKE VPVGDKEAEA PLAP
//
