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Database: UniProt
Entry: J5JJY9_BEAB2
LinkDB: J5JJY9_BEAB2
Original site: J5JJY9_BEAB2 
ID   J5JJY9_BEAB2            Unreviewed;       432 AA.
AC   J5JJY9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Homocysteine synthase {ECO:0000313|EMBL:EJP63596.1};
GN   ORFNames=BBA_07522 {ECO:0000313|EMBL:EJP63596.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP63596.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP63596.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP63596.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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; JH725174; EJP63596.1; -; Genomic_DNA.
DR   RefSeq; XP_008600841.1; XM_008602619.1.
DR   AlphaFoldDB; J5JJY9; -.
DR   STRING; 655819.J5JJY9; -.
DR   GeneID; 19890534; -.
DR   HOGENOM; CLU_018986_4_0_1; -.
DR   InParanoid; J5JJY9; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000002762; 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:UP000002762};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   432 AA;  46530 MW;  59B34A4AEA6D799C CRC64;
     MAEEISKNFE TLQLHAGQEP DPATNARAVP IYATTSFTFK DSAHGARLFG LKEPGNIYSR
     IMNPTVDVFE KRIAALEGGV AGLAASSGQS AQFITINTLA HAGDNIISTS NLYGGTYNQF
     KVFLPRLGIT TKFVNGENPD EIDALIDDKT KAIYVESIGN PRYNVPDLEA IAKVAHAKGV
     PLVVDNTFGA GGYFVRPIDH GADIVVHSAT KWIGGHGTTV GGVIVDSGKF DWGANAARFP
     QFIEPSDGYH GLKFWETFGA LSFIVRARVE IVRDLGAYLN AFAAQQLLLG TETLSLRAER
     HAQNALALAR YLEKSDKVDW VSYPGLASHP SHETAKKYLK RGFGGVLNFG VKGGVAEGAK
     VVDNFKLISN LANVGDAKTL AIHPWSTTHE QLSDEEKTSS GVTEDLIRIS VGVEHIDDII
     ADFEQSFKAA GI
//
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