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Database: UniProt
Entry: A0A2C5X3Z5_9PEZI
LinkDB: A0A2C5X3Z5_9PEZI
Original site: A0A2C5X3Z5_9PEZI 
ID   A0A2C5X3Z5_9PEZI        Unreviewed;       449 AA.
AC   A0A2C5X3Z5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE            EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN   Name=SAH1 {ECO:0000313|EMBL:PHH52712.1};
GN   ORFNames=CFIMG_001970RA {ECO:0000313|EMBL:PHH52712.1};
OS   Ceratocystis fimbriata CBS 114723.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH52712.1, ECO:0000313|Proteomes:UP000222788};
RN   [1] {ECO:0000313|EMBL:PHH52712.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH52712.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA   Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT   "Analysis of microsatellite markers in the genome of the plant pathogen
RT   Ceratocystis fimbriata.";
RL   Fungal Biol. 117:545-555(2013).
RN   [2] {ECO:0000313|EMBL:PHH52712.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH52712.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA   Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT   "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT   the plant pathogen, Ceratocystis fimbriata.";
RL   IMA Fungus 4:357-358(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001109-2,
CC         ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2,
CC       ECO:0000256|RuleBase:RU000548};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|RuleBase:RU000548}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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:PHH52712.1}.
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DR   EMBL; APWK03000059; PHH52712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5X3Z5; -.
DR   STRING; 1035309.A0A2C5X3Z5; -.
DR   OrthoDB; 120477at2759; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000222788; Unassembled WGS sequence.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:RHEA.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00563; AdoHcyase; 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   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 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.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU000548};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU000548};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222788}.
FT   DOMAIN          194..355
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         160..162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         225..230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         302..304
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         349
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         356
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   449 AA;  48630 MW;  596562A18E107E61 CRC64;
     MAAPATVFKV ADLSLAAFGR KEIELAENEM PGLMATRAKY AADQPLKGAR IAGCLHMTIQ
     TAVLIETLVA LGAEVTWSSC NIFSTQDHAA AAIAAAGIPV FAWKGETEEE YNWCLEQQLN
     AFKDGKKLNL ILDDGGDLTQ LVHSKYPEML KDCYGVSEET TTGVHHLYKM LKNGELLVPA
     INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMVAGKIAV VAGFGDVGKG CAMALSTMGA
     RVLVTEIDPI NALQAAMAGY QVTTMDKAAS IGQIFVTTTG CRDILVGKHF EQMPNDAIVC
     NIGHFDIEID VAWLKANAAS VQNIKPQVDR FLMKNGRHLI LLAEGRLVNL GCATGHSSFV
     MSCSFTNQVL AQIQLYKSGD AAFCNKFVEF SKLGKLETGV FVLPKILDEE VARLHLAHCN
     VELTSLTPVQ AEYLGLPVEG PFKADIYRY
//
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