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A1VFZ7 (SAHH_DESVV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:
Adenosylhomocysteinase

EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Short name=AdoHcyase
Gene names
Name:ahcY
Ordered Locus Names:Dvul_2347
OrganismDesulfovibrio vulgaris subsp. vulgaris (strain DP4) [Complete proteome] [HAMAP]
Taxonomic identifier391774 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP MF_00563

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP MF_00563

Cofactor

Binds 1 NAD per subunit By similarity. HAMAP MF_00563

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP MF_00563

Subcellular location

Cytoplasm By similarity HAMAP MF_00563.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024725

Regions

Nucleotide binding204 – 2063NAD By similarity
Nucleotide binding267 – 2726NAD By similarity
Nucleotide binding346 – 3483NAD By similarity

Sites

Binding site661Substrate By similarity
Binding site1421Substrate By similarity
Binding site2031Substrate By similarity
Binding site2331Substrate By similarity
Binding site2371Substrate By similarity
Binding site2381NAD By similarity
Binding site2901NAD By similarity
Binding site3251NAD By similarity
Binding site3941NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VFZ7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 27881713CC2C80B1

FASTA47952,897
        10         20         30         40         50         60 
MTDAKRAQKL DLSLDHKVAD MSLADYGRKD LQLSEREMPG LMELIRKYGG TKPLKGLKVT 

        70         80         90        100        110        120 
GSLHMTIQTA MLIRTLYELG ADIRWASCNI FSTQDHAAAA IAASGMAKVF AWKGETLEDY 

       130        140        150        160        170        180 
WWCTEMALTW PDGSGPDLLV DDGGDATLFI HKGVEVENDP SLLKKAYDNK EFQIIMDRLA 

       190        200        210        220        230        240 
LAYEQDPGRW QRVAAKVRGV SEETTTGVHR LYQLEQEGKL LFPAINVNDA VTKSKFDNLY 

       250        260        270        280        290        300 
GCRESLADGI KRATDVMVAG KVVVVAGYGD VGKGCAQSMR GFGARVLVTE IDPICALQAA 

       310        320        330        340        350        360 
MEGYEVTTME EAVRTGDIFV TATGNCNVIT GAHMEAMKDE AIVCNIGHFD NEIDMHYLEN 

       370        380        390        400        410        420 
TEGCVCLNIK PQVDKWTLRS GRSIIVLAEG RLVNLGCATG HPSFVMSASF TNQTLAQIEL 

       430        440        450        460        470 
ATNPDLERKV YTLPKKLDEE VARLHLDRLG VKLTRLSKDQ ADYIGVSPEG PFKPDHYRY 

« Hide

References

[1]"Contribution of mobile genetic elements to Desulfovibrio vulgaris genome plasticity."
Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P., Stahl D.A.
Environ. Microbiol. 11:2244-2252(2009) [PubMed: 19737303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000527 Genomic DNA. Translation: ABM29363.1.
RefSeqYP_967790.1. NC_008751.1.

3D structure databases

ProteinModelPortalA1VFZ7.
SMRA1VFZ7. Positions 15-479.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VFZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4662413.
GenomeReviewsGene locus Dvul_2347 in contig CP000527_GR.
KEGGdvl:Dvul_2347.
PATRIC21768624. VBIDesVul62463_2578.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBA1VFZ7.
ProtClustDBPRK05476.

Family and domain databases

HAMAPMF_00563. AdoHcyase.
[Tree]
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 nameSAHH_DESVV
AccessionPrimary (citable) accession number: A1VFZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families