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Database: UniProt
Entry: A0A0M8NZL4_9EURO
LinkDB: A0A0M8NZL4_9EURO
Original site: A0A0M8NZL4_9EURO 
ID   A0A0M8NZL4_9EURO        Unreviewed;       436 AA.
AC   A0A0M8NZL4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACN38_g11623 {ECO:0000313|EMBL:KOS37581.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS37581.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS37581.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS37581.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) 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:KOS37581.1}.
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DR   EMBL; LHQQ01000309; KOS37581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8NZL4; -.
DR   STRING; 229535.A0A0M8NZL4; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000037696; 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   Reference proteome {ECO:0000313|Proteomes:UP000037696}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   436 AA;  47180 MW;  1FBDCB4A7A7F8F90 CRC64;
     MSENLHFDTL QLHAGHEPDS ATNSRAVPIY ATSSYVFNDS AHGARLFGLK EFGNLYSRIM
     NPTVDVFEKR IAALEGGVAA VAAASGQAAQ FMAISALAHA GDNIVSTSNL YGGTYNQFKV
     MFPRMGITTK FIQGDKPEDI AAAIDDRTKA VYLESIGNPR YNVPDFEAIA KAAHEKGVPV
     VVDNTFGAGG YFVRPIDHGA DIVVHSATKW IGGHGTTIAG VVIDSGKFDW GKNAARFPQF
     VEPSEGYHGL KFWETFGSLA YAIRVRVEIL RDLGSALNPF AAQQLILGLE TLSLRCERHA
     TNTIALAKWL QKNENVSWVS YPGLEDHPSH DLAKKYLPRG FGGVLSVGIK GGAAAGAQVV
     DNFKLISNLA NVGDSKTLAI HPWSTTHEQL TEQERRDSGV KEDGIRISVG TEYIDDIIAD
     FEQSFQASKA LPDRTA
//
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