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Reviewed, UniProtKB/Swiss-Prot Q04WX0 (SAHH_LEPBL)

Last modified June 16, 2009. Version 21. 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
    EC=3.3.1.1
Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase
      Short name=AdoHcyase
Gene names
Name: ahcY
Ordered Locus Names: LBL_4105
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]
Taxonomic identifier355276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 NAD per subunit By similarity.

Pathway

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

Subcellular location

Cytoplasm By similarity.

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 compound metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: HAMAP

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024730

Regions

Region188 – 356169NAD binding By similarity

Sites

Binding site621Substrate By similarity
Binding site1361Substrate By similarity
Binding site1611Substrate By similarity
Binding site1911Substrate By similarity
Binding site1951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04WX0-1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F4BD8B927CAFC3E1

FASTA43648,096
        10         20         30         40         50         60 
MSATTQEKGL NYKVKDLSQA EWGRQEIILA EKEMPGLMAL RQEYKGKKPL AGARIAGSLH 

        70         80         90        100        110        120 
MTIQTAVLIE TLTELGAEVR WSSCNIFSTQ DHAAAAIAKA GVPVFAWKGE TEEEYWWCIE 

       130        140        150        160        170        180 
QTLFFGDKGP NMILDDGGDL TAYVHEKYPK LLSEIRGISE ETTTGVKSLY KLLKKGELKV 

       190        200        210        220        230        240 
PAFNVNDSVT KSKFDNLYGC RESLADGIKR ATDVMLAGKV ALVCGFGDVG KGSAASLRNF 

       250        260        270        280        290        300 
GARVIVTEID PICALQASME GYQVLRVEDI IEQVDIVVTA TGNDDIITLE HMKAMKDGAI 

       310        320        330        340        350        360 
LCNIGHFDTE IQMSRLNSEK GVTKKEIKPQ VDKYTFPDGK SIVVLAEGRL VNLGCATGHP 

       370        380        390        400        410        420 
SFVMSCSFTN QVLAQIELYN NKYELGVYTL PKHLDEKVAA LHLEQLGVRL TKLNQKQADY 

       430 
LGVPLNGPFK PENYRY 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000349 Genomic DNA. Translation: ABJ80425.1.
RefSeqYP_799358.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4409189.
GenomeReviewsGene locus LBL_4105 in contig CP000349_GR.
KEGGlbl:LBL_4105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ04WX0. HMRAMKD.

Family and domain databases

HAMAPMF_00563.
[Tree]
InterProIPR000043. Ad_hcy_hydrolase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.1480. Ad_hcy_hydrolase. 1 hit.
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_LEPBL
AccessionPrimary (citable) accession number: Q04WX0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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