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Database: UniProt
Entry: F4PEZ3_BATDJ
LinkDB: F4PEZ3_BATDJ
Original site: F4PEZ3_BATDJ 
ID   F4PEZ3_BATDJ            Unreviewed;       430 AA.
AC   F4PEZ3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BATDEDRAFT_14993 {ECO:0000313|EMBL:EGF76195.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF76195.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF76195.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) 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; GL882902; EGF76195.1; -; Genomic_DNA.
DR   RefSeq; XP_006683174.1; XM_006683111.1.
DR   AlphaFoldDB; F4PEZ3; -.
DR   STRING; 684364.F4PEZ3; -.
DR   GeneID; 18236992; -.
DR   HOGENOM; CLU_018986_4_2_1; -.
DR   InParanoid; F4PEZ3; -.
DR   OMA; NAFQIIQ; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000007241; 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:UP000007241}.
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   430 AA;  46571 MW;  04B1C50DE39F8994 CRC64;
     MTNFKPETLL LHGGQQPDPV TGAIAVPIYR TTAYEFQDTV HAQRLFALQK PGNIYSRIMN
     PTVDVFEKRV ALLEKGTAAV ALSSGMAAIA FSILNITRAG DEIIAAGSLY GGTYNLFANT
     LPNYGIKTTF VNETNPENFR AAITEKTKAI FAETVGNPSL NILDIEAVAN IAHEYGLPLI
     VDNTFPSPYG SNPIDFGADV VVHSATKWIG GHGTTIGGVV VDAGKFDWTQ GRFPGFTEPD
     ESYHGLRYGI DTAAAAFATK LRVQLLRDFG PTLSADAAFN FLQGLETLHL RVTKQNENAL
     KVAEYLQNHP SVEYVNYSAF ENFPSHKLAN KYLKNGYGSI LTFGIKGGRE AGSRLIDSVE
     LFSHVANVGD ARSLIIHPAS TTHQQLSAEE LKVAGVFEEL IRLSIGLEAV EDIIADLDQA
     IVKAQQALIL
//
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