ID A0A0F4Z5W8_TALEM Unreviewed; 380 AA.
AC A0A0F4Z5W8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:KKA25496.1};
GN ORFNames=T310_0450 {ECO:0000313|EMBL:KKA25496.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25496.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA25496.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25496.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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:KKA25496.1}.
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DR EMBL; LASV01000019; KKA25496.1; -; Genomic_DNA.
DR RefSeq; XP_013332108.1; XM_013476654.1.
DR AlphaFoldDB; A0A0F4Z5W8; -.
DR STRING; 1408163.A0A0F4Z5W8; -.
DR GeneID; 25312504; -.
DR OrthoDB; 1779220at2759; -.
DR Proteomes; UP000053958; 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 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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KKA25496.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482259"
SQ SEQUENCE 380 AA; 41783 MW; 92341A3C90A5C9FE CRC64;
MSIREQALSL SLFSLLLPSS STAVPMEQTF LLGERRRMLT VGWRTSGQAA RWMAIAGLAA
ASDNIVSAST ISEEAYTQFR YRFPSQGISV KFIDVEDADV LRNAIDDRTK AVYVESLSPP
HPVIASIHIL TLCRDNTPGA GGYLCRPIDH GADIVIHSAS ERLGGLGHAI AGAIVDSGKF
PWNVHARRFL HLTEPAPGYH GMKFWEKFGD KAYIFYVRSA LLRDAGPCLN PFAAFSLLAG
METLSVRMDR HSGNALALAR WLEGHEKVAW VVYPGLPSHP SFERAKRYLR NGFGGLLFFR
LAAGDEASQA AMRKFKLVRN ADGIGTTQTL VHYHRVATGS YVQESPSQQS DHNTAAMRVS
VGLEHIDDII EDFRQALACV
//
