ID A0A024UNU8_9STRA Unreviewed; 392 AA.
AC A0A024UNU8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_02340 {ECO:0000313|EMBL:ETW07954.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07954.1};
RN [1] {ECO:0000313|EMBL:ETW07954.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07954.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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; KI913954; ETW07954.1; -; Genomic_DNA.
DR RefSeq; XP_008864047.1; XM_008865825.1.
DR AlphaFoldDB; A0A024UNU8; -.
DR STRING; 157072.A0A024UNU8; -.
DR EnsemblFungi; H310_02340-t26_1; H310_02340-t26_1-p1; H310_02340.
DR EnsemblProtists; ETW07954; ETW07954; H310_02340.
DR GeneID; 20079390; -.
DR VEuPathDB; FungiDB:H310_02340; -.
DR eggNOG; KOG0053; Eukaryota.
DR OrthoDB; 6018at2759; -.
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}.
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 392 AA; 41963 MW; 0119071A2E3ACA81 CRC64;
MTDYTTLQVH AGHEGGEPGS RARAVPIVAS TSFLFDNADH AGKLFGLQEF GNIYSRIMNP
TNDVFEKRVT ALSGGVASVA VSSGQAAQAL TIFTIAQAGD NIVATSSLYG GTYNQFKVAF
PRLGIQVKFA NHADPASIRS LIDDKTKAIY VETIGNPELE VPDFDAISAI AKEHEIPFIV
DDTFGACGYL VNPIKHGADI VVQSATKWIG GHGTTIGGVV TDAGTFNWGN GKFPMMSEPS
PGYHGLNFWK VFGPGGVLGA NATFAIRLRV ENLRDFGSSL SPFNSFLLIQ GLETLSLRVD
RAADNALTLA QWLETHPNVA WVSYPGLPSH PSHENAKKYM YRKKYGAVLT FGVKGGLEAG
RSFINSVKLA SHLANVGDSK TLSNRRRASS PT
//
