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Reviewed, UniProtKB/Swiss-Prot P93253 (SAHH_MESCR)

Last modified November 24, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier3544 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAizoaceaeMesembryanthemum

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Adenosylhomocysteinase
PRO_0000116926

Regions

Region232 – 401170NAD binding By similarity

Sites

Binding site641Substrate By similarity
Binding site1391Substrate By similarity
Binding site2051Substrate By similarity
Binding site2351Substrate By similarity
Binding site2391Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P93253-1 [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 

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References

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

Cross-references

Sequence databases

U79766 mRNA. Translation: AAB38499.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.3.1.1. 2210.

Family and domain databases

InterProIPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR000043. S-Ado-L-homoCys_hydrolase.
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.
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: November 24, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents