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Database: UniProt
Entry: A0A081CK25_PSEA2
LinkDB: A0A081CK25_PSEA2
Original site: A0A081CK25_PSEA2 
ID   A0A081CK25_PSEA2        Unreviewed;       446 AA.
AC   A0A081CK25;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=O-acetylhomoserine (Thiol)-lyase-like protein {ECO:0000313|EMBL:GAK67021.1};
DE   SubName: Full=Probable O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:SPO48267.1};
GN   ORFNames=PAN0_016c5247 {ECO:0000313|EMBL:GAK67021.1}, PSANT_05956
GN   {ECO:0000313|EMBL:SPO48267.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK67021.1, ECO:0000313|Proteomes:UP000053758};
RN   [1] {ECO:0000313|Proteomes:UP000053758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA   Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA   Morita T.;
RT   "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT   JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT   Lipids.";
RL   Genome Announc. 2:e00878-e00814(2014).
RN   [2] {ECO:0000313|EMBL:GAK67021.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK67021.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SPO48267.1, ECO:0000313|Proteomes:UP000325008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC   {ECO:0000313|EMBL:SPO48267.1};
RA   Guldener U.;
RL   Submitted (MAR-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}.
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DR   EMBL; DF830083; GAK67021.1; -; Genomic_DNA.
DR   EMBL; OOIQ01000018; SPO48267.1; -; Genomic_DNA.
DR   RefSeq; XP_014654674.1; XM_014799188.1.
DR   AlphaFoldDB; A0A081CK25; -.
DR   GeneID; 26306049; -.
DR   HOGENOM; CLU_018986_4_0_1; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000053758; Unassembled WGS sequence.
DR   Proteomes; UP000325008; 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:GAK67021.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT   REGION          426..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   446 AA;  47519 MW;  EC7C20FC0151464E CRC64;
     MSHFDTLQLH AGQEVDPATN ALAVPIYANS SFAFNDSAHG ADLFGLRKFG NIYSRLMNPT
     NDVFEKRMAA LEGGAAALAT SSGQAAQGMV VMGLAGAGDN IVSSSYLYGG TYNAWANLFP
     RLGITTKFVK SEKPEDYAAA IDAKTKAIYI ESIANPKYIV HDIAAIAKVA HDHGIPLVVD
     NTFGAGGYLV RPIEHGADIV VHSATKWIGG HGTTIGGVIV DSGKFDWSKS GKFPQFTEPS
     AGYHGLKFWD TFGPITFAIY LRVVILRDLG PCQNPFGSFL LLQGLETLSL RVGRIVENAL
     SLAKWLEQHP QVSWVSYPGL ESHPSHETAK KYLQRGFGGV LSFGIKGDAA KGSAFVDSLK
     LATNLANVGD AKTLIIHPAS TTHQQLSDED QLSSGVTKDL IRVSVGYEWI EDIKADFTQA
     FEKTSGVKGD VSSGQTGPAP GLSGSV
//
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