SAHH_CAEEL
ID SAHH_CAEEL Reviewed; 437 AA.
AC P27604;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=Protein dumpy-14;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=ahcy-1; Synonyms=ahh, dpy-14; ORFNames=K02F2.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8458573; DOI=10.1139/g93-008;
RA Prasad S.S., Starr T., Rose A.M.;
RT "Molecular characterization in the dpy-14 region identifies the
RT adenosylhomocysteine hydrolase gene in Caenorhabditis elegans.";
RL Genome 36:57-65(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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.
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=3.3.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; M64306; AAA28062.1; -; Genomic_DNA.
DR EMBL; S57284; AAB25906.1; -; Genomic_DNA.
DR EMBL; FO081029; CCD68626.1; -; Genomic_DNA.
DR PIR; T32918; T32918.
DR RefSeq; NP_491955.1; NM_059554.6.
DR AlphaFoldDB; P27604; -.
DR SMR; P27604; -.
DR BioGRID; 37854; 48.
DR DIP; DIP-25388N; -.
DR IntAct; P27604; 1.
DR STRING; 6239.K02F2.2.2; -.
DR iPTMnet; P27604; -.
DR World-2DPAGE; 0011:P27604; -.
DR World-2DPAGE; 0020:P27604; -.
DR EPD; P27604; -.
DR PaxDb; P27604; -.
DR PeptideAtlas; P27604; -.
DR EnsemblMetazoa; K02F2.2.1; K02F2.2.1; WBGene00019322.
DR GeneID; 172408; -.
DR KEGG; cel:CELE_K02F2.2; -.
DR UCSC; K02F2.2.1; c. elegans.
DR CTD; 172408; -.
DR WormBase; K02F2.2; CE17154; WBGene00019322; ahcy-1.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; P27604; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; P27604; -.
DR Reactome; R-CEL-156581; Methylation.
DR Reactome; R-CEL-1614635; Sulfur amino acid metabolism.
DR SignaLink; P27604; -.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:P27604; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019322; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:WormBase.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:WormBase.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; ISS:WormBase.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 2.
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 PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 2.
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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..437
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116910"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224..229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 301..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 47536 MW; 53ADAB24507CFCD6 CRC64;
MAQSKPAYKV ADIKLADFGR KEIILAENEM PGLMAMRSKY GPSQPLKGAR IAGCLHMTIQ
TAVLIETLTA LGAEVQWSSC NIFSTQDHAA AAIAQTGVPV YAWKGETDEE YEWCIEQTIV
FKDGQPLNMI LDDGGDLTNL VHAKYPQYLA GIRGLSEETT TGVHNLAKML AKGDLKVPAI
NVNDSVTKSK FDNLYGIRES LPDGIKRATD VMLAGKVAVV AGYGDVGKGS AASLKAFGSR
VIVTEIDPIN ALQAAMEGYE VTTLEEAAPK ANIIVTTTGC KDIVTGKHFE LLPNDAIVCN
VGHFDCEIDV KWLNTNATKK DTIKPQVDRY TLKNGRHVIL LAEGRLVNLG CATGHPSFVM
SNSFTNQVLA QVELWTKFGT PQEYKLGLYV LPKTLDEEVA YLHLAQLGVK LTKLSDEQAS
YLGVPVAGPY KPDHYRY
