ID K9R3H9_9LAMI Unreviewed; 109 AA.
AC K9R3H9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|ARBA:ARBA00022091};
DE EC=3.13.2.1 {ECO:0000256|ARBA:ARBA00034527};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|ARBA:ARBA00033091};
DE Flags: Fragment;
GN Name=SAHH {ECO:0000313|EMBL:AFY52435.1};
OS Cyrtandra lysiosepala.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae;
OC Didymocarpinae; Cyrtandra.
OX NCBI_TaxID=1263649 {ECO:0000313|EMBL:AFY52435.1};
RN [1] {ECO:0000313|EMBL:AFY52435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G202 {ECO:0000313|EMBL:AFY52435.1};
RX PubMed=23394592; DOI=10.1186/1471-2148-13-35;
RA Pillon Y., Johansen J., Sakishima T., Chamala S., Barbazuk W.B.,
RA Roalson E.H., Stacy E.A.;
RT "Potential use of low-copy nuclear genes in DNA barcoding: a comparison
RT with plastid genes in two Hawaiian plant radiations.";
RL BMC Evol. Biol. 13:35-35(2013).
CC -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC adenosyl-L-methionine-dependent methyl transferase reactions; therefore
CC adenosylhomocysteinase may play a key role in the control of
CC methylations via regulation of the intracellular concentration of
CC adenosylhomocysteine. {ECO:0000256|ARBA:ARBA00002639}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005195}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122}.
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DR EMBL; JX846005; AFY52435.1; -; Genomic_DNA.
DR UniPathway; UPA00314; UER00076.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; PF00670; AdoHcyase_NAD; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AFY52435.1}.
FT DOMAIN 1..105
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFY52435.1"
FT NON_TER 109
FT /evidence="ECO:0000313|EMBL:AFY52435.1"
SQ SEQUENCE 109 AA; 12101 MW; 0CB73E5EED4DFC52 CRC64;
LQALMEGYQV LTLXDVVSEA DIFVTTTGNK DIIMVDHMKK MKNNAIVCNI GHFDNEIDXL
GLETYPGIKK ITIKPQTDRW VFPETKSGII ILAEGRLMNL GCATGHPSF
//
