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UniProtKB/Swiss-Prot entry P10760


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SAHH_RAT
Primary accession number P10760
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name Adenosylhomocysteinase
Synonyms AdoHcyase
EC 3.3.1.1
S-adenosyl-L-homocysteine hydrolase
Gene name
Name: Ahcy
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3027698 [NCBI, ExPASy, EBI, Israel, Japan]
Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund P.S. Jr., Aksamit R.R., Unson C.G., Cantoni G.L.;
"Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence.";
Proc. Natl. Acad. Sci. U.S.A. 84:719-723(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Fischer 344;
PubMed=7744082 [NCBI, ExPASy, EBI, Israel, Japan]
Merta A., Aksamit R.R., Kasir J., Cantoni G.L.;
"The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase.";
Eur. J. Biochem. 229:575-582(1995).
[3]
PROTEIN SEQUENCE OF 76-94.
PubMed=3759971 [NCBI, ExPASy, EBI, Israel, Japan]
Gomi T., Ogawa H., Fujioka M.;
"S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5'-p-fluorosulfonylbenzoyladenosine.";
J. Biol. Chem. 261:13422-13425(1986).
[4]
PROTEIN SEQUENCE OF 143-151 AND 268-285, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W.;
Submitted (APR-2007) to UniProtKB.
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
TISSUE=Liver;
DOI=10.1021/bi990332k; PubMed=10387078 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.;
"Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.";
Biochemistry 38:8323-8333(1999).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245.
DOI=10.1074/jbc.M003725200; PubMed=10913437 [NCBI, ExPASy, EBI, Israel, Japan]
Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.;
"Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure of D244E mutant enzyme.";
J. Biol. Chem. 275:32147-32156(2000).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
DOI=10.1074/jbc.M109187200; PubMed=11741948 [NCBI, ExPASy, EBI, Israel, Japan]
Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., Fujioka M., Takusagawa F.;
"Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine hydrolase complexed with D-eritadenine.";
J. Biol. Chem. 277:7477-7482(2002).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF ASP-131; LYS-186; ASP-190 AND ASN-191.
DOI=10.1074/jbc.M201116200; PubMed=11927587 [NCBI, ExPASy, EBI, Israel, Japan]
Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M., Takusagawa F.;
"Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.";
J. Biol. Chem. 277:22670-22676(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M15185; AAA40705.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14937; AAA92043.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26583; A26583.
RefSeq NP_058897.1; -.
UniGene Rn.5878
3D structure databases
PDB
1B3R; X-ray; 2.80 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
1D4F; X-ray; 2.80 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
1K0U; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-432.[ExPASy / RCSB / EBI]
1KY4; X-ray; 2.80 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
1KY5; X-ray; 2.80 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
1XWF; X-ray; 2.80 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
2H5L; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-432.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B3R; -.
1D4F; -.
1K0U; -.
1KY4; -.
1KY5; -.
1XWF; -.
2H5L; -.
ModBase P10760.
Enzyme and pathway databases
BioCyc MetaCyc:MON-8582; -.
Organism-specific databases
RGD 69260; Ahcy.
Gene expression databases
ArrayExpress P10760; -.
GermOnline ENSRNOG00000017777; Rattus norvegicus.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004013; Molecular function: adenosylhomocysteinase activity (inferred from electronic annotation from InterPro).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000043; Ad_hcy_hydrolase.
IPR015878; Ado_hCys_hydrolase_NAD-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1.
PANTHER PTHR23420; Ad_hcy_hydrolase; 1.
Pfam PF05221; AdoHcyase; 1.
PF00670; AdoHcyase_NAD; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001109; Ad_hcy_hydrolase; 1.
TIGRFAMs TIGR00936; ahcY; 1.
PROSITE PS00738; ADOHCYASE_1; 1.
PS00739; ADOHCYASE_2; 1.
Genome annotation databases
Ensembl ENSRNOG00000017777; Rattus norvegicus. [Contig view]
GeneID 29443; -.
KEGG rno:29443; -.
NMPDR fig|10116.3.peg.20074; -.
Phylogenomic databases
HOVERGEN P10760; -.
Other
LinkHub P10760; -.
NextBio 609197; -.
ProtoNet P10760.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; NAD; One-carbon metabolism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   432  431     Adenosylhomocysteinase. PRO_0000116905
REGION   183   350  168     NAD binding. 
BINDING   57    57        Substrate. 
BINDING   131   131        Substrate. 
BINDING   156   156        Substrate. 
BINDING   186   186        Substrate. 
BINDING   190   190        Substrate. 
MUTAGEN   131   131        D->N: Strongly reduces activity. 
MUTAGEN   186   186        K->N: Strongly reduces activity. 
MUTAGEN   190   190        D->N: Strongly reduces activity. 
MUTAGEN   191   191        N->S: Strongly reduces activity. 
MUTAGEN   245   245        D->E: Changes active site geometry and alters affinity for NAD. 
STRAND   8    10  3      
TURN   12    14  3      
HELIX   15    25  11      
HELIX   26    28  3      
HELIX   30    39  10      
TURN   40    42  3      
TURN   44    47  4      
STRAND   49    54  6      
HELIX   58    69  12      
STRAND   73    77  5      
TURN   81    83  3      
HELIX   86    94  9      
STRAND   99   101  3      
HELIX   107   116  10      
STRAND   127   133  7      
HELIX   134   142  9      
HELIX   144   147  4      
STRAND   152   155  4      
HELIX   158   169  12      
STRAND   177   179  3      
HELIX   184   190  7      
HELIX   192   207  16      
STRAND   215   219  5      
HELIX   223   234  12      
STRAND   238   242  5      
HELIX   246   253  8      
TURN   254   256  3      
STRAND   258   260  3      
HELIX   262   265  4      
TURN   266   268  3      
STRAND   270   274  5      
STRAND   277   279  3      
HELIX   284   287  4      
STRAND   294   298  5      
TURN   302   304  3      
HELIX   308   314  7      
STRAND   315   322  8      
STRAND   325   330  6      
STRAND   335   339  5      
HELIX   340   342  3      
HELIX   345   349  5      
HELIX   355   374  20      
TURN   376   378  3      
STRAND   381   385  5      
HELIX   388   398  11      
TURN   399   402  4      
HELIX   411   417  7      
STRAND   421   423  3      
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 47538 Da [This is the MW of the unprocessed precursor] CRC64: 93CA5BED07B4FCDE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET 

        70         80         90        100        110        120 
AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY LWCIEQTLHF 

       130        140        150        160        170        180 
KDGPLNMILD DGGDLTNLIH TKHPQLLSGI RGISEETTTG VHNLYKMMAN GILKVPAINV 

       190        200        210        220        230        240 
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI 

       250        260        270        280        290        300 
ITEIDPINAL QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG 

       310        320        330        340        350        360 
HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA MGHPSFVMSN 

       370        380        390        400        410        420 
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMP 

       430 
INGPFKPDHY RY 

P10760 in FASTA format

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