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B2AGG2 (SAHH_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Short name=AdoHcyase
Gene names
Name:ahcY
Ordered Locus Names:RALTA_A0188
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length472 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 – 472472Adenosylhomocysteinase HAMAP MF_00563
PRO_1000129280

Regions

Nucleotide binding197 – 1993NAD By similarity
Nucleotide binding260 – 2656NAD By similarity
Nucleotide binding339 – 3413NAD By similarity

Sites

Binding site611Substrate By similarity
Binding site1361Substrate By similarity
Binding site1961Substrate By similarity
Binding site2261Substrate By similarity
Binding site2301Substrate By similarity
Binding site2311NAD By similarity
Binding site2831NAD By similarity
Binding site3181NAD By similarity
Binding site3841NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B2AGG2 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 21D807EC34110B95

FASTA47251,913
        10         20         30         40         50         60 
MNAVTDLKQD YLVADINLAG WGRKEIAIAE TEMPGLMAIR DEFAAAQPLK GARIAGSLHM 

        70         80         90        100        110        120 
TIQTAVLIET LKALGADVRW ASCNIFSTQD HAAAAIAAGG TPVFAFKGES LKEYWDFTHR 

       130        140        150        160        170        180 
IFDWADGGTP NMILDDGGDA TLLLHLGARA EKDQSVIANP GSEEETFLFA AIKEKLAKDP 

       190        200        210        220        230        240 
SWYSRNLAAI RGVTEETTTG VHRLYQMAQK GELRFPAINV NDSVTKSKFD NLYGCRESLV 

       250        260        270        280        290        300 
DGIKRATDVM IAGKIAVVAG YGDVGKGSAQ ALRALSAQVW VTEIDPICAL QAAMEGYRVV 

       310        320        330        340        350        360 
TMDYAAEHGD IFVTCTGNYH VITHEHMAKM KDQAIVCNIG HFDNEIDIAS IEKYEWDEIK 

       370        380        390        400        410        420 
PQVDHVKFPD GKKLIILAKG RLVNLGCATG HPSYVMSSSF ANQTIAQIEL WQERDSGKYP 

       430        440        450        460        470 
VGVYTLPKHL DEKVARLQLR KLNAQLTELT DQQAAYIGVK KEGPYKADHY RY

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAP62861.1.
RefSeqYP_001795583.1. NC_010528.1.

3D structure databases

ProteinModelPortalB2AGG2.
SMRB2AGG2. Positions 9-472.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2AGG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6301696.
GenomeReviewsGene locus RALTA_A0188 in contig CU633749_GR.
KEGGcti:RALTA_A0188.
PATRIC21527008. VBICupTai42494_0190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
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_CUPTR
AccessionPrimary (citable) accession number: B2AGG2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 30 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

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