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Database: UniProt
Entry: A0A2I0WD38_9ASPA
LinkDB: A0A2I0WD38_9ASPA
Original site: A0A2I0WD38_9ASPA 
ID   A0A2I0WD38_9ASPA        Unreviewed;       426 AA.
AC   A0A2I0WD38;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|ARBA:ARBA00034527, ECO:0000256|RuleBase:RU000548};
DE            EC=3.13.2.1 {ECO:0000256|ARBA:ARBA00034527, ECO:0000256|RuleBase:RU000548};
GN   Name=SAHH {ECO:0000313|EMBL:PKU73569.1};
GN   ORFNames=MA16_Dca023681 {ECO:0000313|EMBL:PKU73569.1};
OS   Dendrobium catenatum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU73569.1, ECO:0000313|Proteomes:UP000233837};
RN   [1] {ECO:0000313|EMBL:PKU73569.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU73569.1};
RX   PubMed=26754549; DOI=10.1038/srep19029;
RA   Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA   Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA   Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA   Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA   Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA   Liu Z.J.;
RT   "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT   polysaccharide synthase, floral development and adaptive evolution.";
RL   Sci. Rep. 6:19029-19029(2016).
RN   [2] {ECO:0000313|EMBL:PKU73569.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU73569.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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|ARBA:ARBA00034436,
CC         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|ARBA:ARBA00005195, ECO:0000256|RuleBase:RU000548}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR   EMBL; KZ502738; PKU73569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0WD38; -.
DR   STRING; 906689.A0A2I0WD38; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000233837; 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; 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   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF28; 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:UP000233837};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..426
FT                   /note="Adenosylhomocysteinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014182291"
FT   DOMAIN          181..344
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         147..149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         212..217
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         289..291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         338
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         345
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   426 AA;  46719 MW;  0751668A07D4B7FA CRC64;
     MNILTIFTFF PLLLMTALGA EVRWCSCNIF STQDHAAAAI ARDSAAVFAW KGETLQEYWW
     CTERCLEWGA GGGPDLIVDD GGDATLLIHE GVKAEEEYEK TGKLPDPAST DNAEFQLVLG
     LIRDSIKVDP KKYSKMKERL VGVSEETTTG VKRLYQMQIS GSLLFPAINV NDSVTKSKFD
     NLYGCRHSLP DGLMRATDVM LAGKVAVVCG YGDVGKGCAA ALKSAGARVI VTEIDPICAL
     QALMEGIPVL TLEDVVADSD IFVTTTGNKD IIMVDHMKKM KNNAIVCNIG HFDNEIDMLG
     LEALPGIKRI TIKPQTDRWV FPDTNKGIIV LAEGRLMNLG CATGHPSFVM SCSFTNQVIA
     QLELWNERSS GKYEKKVYVL PKHLDEKVAL LHLGKLGAKL TKLSPAQAEY ISVPVEGPYK
     PPHYRY
//
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