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P93253 (SAHH_MESCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SAHH
OrganismMesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum)
Taxonomic identifier3544 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Aizoaceae › Mesembryanthemum

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 NAD per subunit.

Pathway

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

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNAD
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Adenosylhomocysteinase
PRO_0000116926

Regions

Nucleotide binding206 – 2083NAD By similarity
Nucleotide binding269 – 2746NAD By similarity
Nucleotide binding348 – 3503NAD By similarity

Sites

Binding site641Substrate By similarity
Binding site1391Substrate By similarity
Binding site2051Substrate By similarity
Binding site2351Substrate By similarity
Binding site2391Substrate By similarity
Binding site2401NAD By similarity
Binding site2921NAD By similarity
Binding site3271NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P93253 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 2C3B339BD4F7BAE6

FASTA48553,178
        10         20         30         40         50         60 
MALAVEKTSS GREYKVKDMS QADFGRLEIE LAEVEMPGLM ACRTEFGPSQ PFKGAKITGS 

        70         80         90        100        110        120 
LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC 

       130        140        150        160        170        180 
TERALDWGAG GGPDLIVDDG GDATLLIHEG VKAEEEYEKN GTIPDPTSTD NPEFQLVLGL 

       190        200        210        220        230        240 
IRDSLKVDPK RYHKMKTRLV GVSEETTTGV KRLYQMQATG TLLFPAINVN DSVTKSKFDN 

       250        260        270        280        290        300 
LYGCRHSLPD GLMRATDVMI AGKVGVVCGY GDVGKGCALA LKAAGARVIV TEIDPICALQ 

       310        320        330        340        350        360 
ALMEGFQILT LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL 

       370        380        390        400        410        420 
ENYPGVKRIT IKPQTDRFVF PETNTGIIVL AEGRLMKLGC ATGHPSFVMS CSFTNQVIAQ 

       430        440        450        460        470        480 
LELWNERASG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLSKDQADYI SVPVEGPYKP 


AHYRY

« Hide

References

[1]Michalowski C.B., Bohnert H.J.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U79766 mRNA. Translation: AAB38499.1.

3D structure databases

ProteinModelPortalP93253.
SMRP93253. Positions 12-485.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. Ad_hcy_hydrolase. 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...

Entry information

Entry nameSAHH_MESCR
AccessionPrimary (citable) accession number: P93253
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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