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Database: UniProt
Entry: S4W9A7_9ASCO
LinkDB: S4W9A7_9ASCO
Original site: S4W9A7_9ASCO 
ID   S4W9A7_9ASCO            Unreviewed;       259 AA.
AC   S4W9A7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Homocysteine hydrolase {ECO:0000313|EMBL:AGO87575.1};
DE   Flags: Fragment;
GN   Name=SAH1 {ECO:0000313|EMBL:AGO87575.1};
OS   Dipodascus armillariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Dipodascus.
OX   NCBI_TaxID=43962 {ECO:0000313|EMBL:AGO87575.1};
RN   [1] {ECO:0000313|EMBL:AGO87575.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 817.71 {ECO:0000313|EMBL:AGO87575.1};
RX   PubMed=23786589; DOI=10.1111/1567-1364.12059;
RA   Koufopanou V., Swire J., Lomas S., Burt A.;
RT   "Primers for fourteen protein-coding genes and the deep phylogeny of the
RT   true yeasts.";
RL   FEMS Yeast Res. 13:574-584(2013).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122}.
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DR   EMBL; KF042691; AGO87575.1; -; Genomic_DNA.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AGO87575.1}.
FT   DOMAIN          120..259
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGO87575.1"
FT   NON_TER         259
FT                   /evidence="ECO:0000313|EMBL:AGO87575.1"
SQ   SEQUENCE   259 AA;  28295 MW;  178C7EE9B40F9FE5 CRC64;
     VTWSSCXIFS TQDHAAAAIA AAGIPVFAWK GETEEEYLWC IEQQLKAFKD DKQLNLILDD
     GGDLTTLVHE KFPELLKDCY GVSEETTTGV HHLYRMLKDG KLKVPAINVN DSVTKSKFDN
     LYGCRESLVD GIKRATDVMI AGKTAVVAGF GDVGKGCAXA LQXMGARVLV TEIDPINALQ
     AAVSGYQVLP MEEACKXGQI FVTTTGCRDI ITGEHFSQMP NDAIVCNIGH FDIEIDVAWL
     KANAKSVVNI KPQVDRYLH
//
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