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Q5R889 (SAHH3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Putative adenosylhomocysteinase 3

Short name=AdoHcyase 3
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase 3
S-adenosylhomocysteine hydrolase-like protein 2
Gene names
Name:AHCYL2
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 NAD per subunit By similarity.

Pathway

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

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNAD
   Molecular functionHydrolase
   PTMPhosphoprotein
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 – 508508Putative adenosylhomocysteinase 3
PRO_0000230302

Regions

Nucleotide binding233 – 2353NAD By similarity
Nucleotide binding298 – 3036NAD By similarity
Nucleotide binding375 – 3773NAD By similarity

Sites

Binding site1331Substrate By similarity
Binding site2071Substrate By similarity
Binding site2321Substrate By similarity
Binding site2621Substrate By similarity
Binding site2661Substrate By similarity
Binding site2671NAD By similarity
Binding site3191NAD By similarity
Binding site3541NAD By similarity
Binding site4221NAD By similarity

Amino acid modifications

Modified residue41Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R889 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A59869443CC8F707

FASTA50856,679
        10         20         30         40         50         60 
MLGSKKKYIV NGNSGIKAQI QFADQKQEFN KRPTKIGRRS LSRSISQSST DSYSSAASYT 

        70         80         90        100        110        120 
DSSDDETSPR DKQQKNSKGS SDFCVKNIKQ AEFGRREIEI AEQEMPALMA LRKRAQGEKP 

       130        140        150        160        170        180 
LAGAKIVGCT HITAQTAVLM ETLGALGAQC RWAACNIYST LNEVAAALAE SGFPVFAWKG 

       190        200        210        220        230        240 
ESEDDFWWCI DRCVNVEGWQ PNMILDDGGD LTHWIYKKYP NMFKKIKGIV EESVTGVHRL 

       250        260        270        280        290        300 
YQLSKAGKLC VPAMNVNDSV TKQKFDNLYC CRESILDGLK RTTDMMFGGK QVVVCGYGEV 

       310        320        330        340        350        360 
GKGCCAALKA MGSIVYVTEI DPICALQACM DGFRLVKLNE VIRQVDIVIT CTGNKNVVTR 

       370        380        390        400        410        420 
EHLDRMKNSC IVCNIGHSNT EIDVASLRTP ELTWERVRSQ VDHVIWPDGK RIVLLAEGRL 

       430        440        450        460        470        480 
LNLSCSTVPT FVLSITATTQ ALALIELYNA PEGRYKQDVY LLPKKMDEYV ASLHLPTFDA 

       490        500 
HLTELTDEQA KYLGLNKNGP FKPNYYRY 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859865 mRNA. Translation: CAH92021.1.
RefSeqNP_001126174.1. NM_001132702.1.
UniGenePab.9439.

3D structure databases

ProteinModelPortalQ5R889.
SMRQ5R889. Positions 80-508.
ModBaseSearch...

Proteomic databases

PRIDEQ5R889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173136.
KEGGpon:100173136.

Organism-specific databases

CTD23382.

Phylogenomic databases

HOVERGENHBG005041.

Family and domain databases

InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
KOK01251.
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 nameSAHH3_PONAB
AccessionPrimary (citable) accession number: Q5R889
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 21, 2004
Last modified: January 25, 2012
This is version 48 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families