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
//