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P10760 (SAHH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Gene names
Name:Ahcy
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit. Ref.5

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Subunit structure

Homotetramer. Ref.5

Subcellular location

Cytoplasm. Melanosome By similarity.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 432431Adenosylhomocysteinase
PRO_0000116905

Regions

Nucleotide binding157 – 1593NAD
Nucleotide binding222 – 2276NAD
Nucleotide binding299 – 3013NAD
Nucleotide binding426 – 4305NAD

Sites

Binding site571Substrate
Binding site1311Substrate
Binding site1561Substrate
Binding site1861Substrate
Binding site1901Substrate
Binding site2431NAD
Binding site2481NAD
Binding site3461NAD
Binding site3531NAD

Experimental info

Mutagenesis1311D → N: Strongly reduces activity. Ref.8
Mutagenesis1861K → N: Strongly reduces activity. Ref.8
Mutagenesis1901D → N: Strongly reduces activity. Ref.8
Mutagenesis1911N → S: Strongly reduces activity. Ref.8
Mutagenesis2451D → E: Changes active site geometry and alters affinity for NAD.

Secondary structure

1 ........................................................................................... 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10760 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 93CA5BED07B4FCDE

FASTA43247,538
        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

« Hide

References

[1]"Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence."
Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund P.S. Jr., Aksamit R.R., Unson C.G., Cantoni G.L.
Proc. Natl. Acad. Sci. U.S.A. 84:719-723(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase."
Merta A., Aksamit R.R., Kasir J., Cantoni G.L.
Eur. J. Biochem. 229:575-582(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Fischer 344.
[3]"S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5'-p-fluorosulfonylbenzoyladenosine."
Gomi T., Ogawa H., Fujioka M.
J. Biol. Chem. 261:13422-13425(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 76-94.
[4]Lubec G., Afjehi-Sadat L., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 143-151 AND 268-285, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[5]"Crystal structure of S-adenosylhomocysteine hydrolase from rat liver."
Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.
Biochemistry 38:8323-8333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, SUBUNIT.
Tissue: Liver.
[6]"Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure of D244E mutant enzyme."
Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.
J. Biol. Chem. 275:32147-32156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245.
[7]"Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine hydrolase complexed with D-eritadenine."
Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., Fujioka M., Takusagawa F.
J. Biol. Chem. 277:7477-7482(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[8]"Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190."
Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M., Takusagawa F.
J. Biol. Chem. 277:22670-22676(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF ASP-131; LYS-186; ASP-190 AND ASN-191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M15185 mRNA. Translation: AAA40705.1.
U14937 Genomic DNA. Translation: AAA92043.1.
IPIIPI00476295.
PIRA26583.
RefSeqNP_058897.1. NM_017201.1.
UniGeneRn.5878.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3RX-ray2.80A/B/C/D2-432[»]
1D4FX-ray2.80A/B/C/D2-432[»]
1K0UX-ray3.00A/B/C/D/E/F/G/H2-432[»]
1KY4X-ray2.80A/B/C/D2-432[»]
1KY5X-ray2.80A/B/C/D2-432[»]
1XWFX-ray2.80A/B/C/D2-431[»]
2H5LX-ray2.80A/B/C/D/E/F/G/H2-431[»]
ProteinModelPortalP10760.
SMRP10760. Positions 3-432.
ModBaseSearch...

Protein-protein interaction databases

IntActP10760. 1 interaction.
MINTMINT-4570399.
STRING10116.ENSRNOP00000024310.

PTM databases

PhosphoSiteP10760.

2D gel databases

World-2DPAGE0004:P10760.

Proteomic databases

PaxDbP10760.
PRIDEP10760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024310; ENSRNOP00000024310; ENSRNOG00000017777.
GeneID29443.
KEGGrno:29443.
UCSCRGD:69260. rat.

Organism-specific databases

CTD191.
RGD69260. Ahcy.

Phylogenomic databases

eggNOGCOG0499.
GeneTreeENSGT00390000003626.
HOGENOMHOG000227987.
HOVERGENHBG005041.
InParanoidP10760.
KOK01251.
OMATIGMALH.
OrthoDBEOG4MW862.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-8582.
BRENDA3.3.1.1. 5301.
SABIO-RKP10760.
UniPathwayUPA00314; UER00076.

Gene expression databases

GenevestigatorP10760.
GermOnlineENSRNOG00000017777. Rattus norvegicus.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. PTHR23420. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP10760.
ChEMBLCHEMBL3118.
EvolutionaryTraceP10760.
NextBio609197.

Entry information

Entry nameSAHH_RAT
AccessionPrimary (citable) accession number: P10760
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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