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Reviewed, UniProtKB/Swiss-Prot Q7NZF7 (SAHH_CHRVO)

Last modified February 9, 2010. Version 51. 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

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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: CV_0965
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

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Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

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.

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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: 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116957

Regions

Region219 – 384166NAD binding By similarity

Sites

Binding site571Substrate By similarity
Binding site1321Substrate By similarity
Binding site1921Substrate By similarity
Binding site2221Substrate By similarity
Binding site2261Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7NZF7-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 5301EBA3D2D5675D

FASTA46651,456
        10         20         30         40         50         60 
MADFSDFHVA DIALAGWGRK ELNIAETEMP GLMATRDEYH AAQPLRGARI AGSLHMTVQT 

        70         80         90        100        110        120 
AVLIETLTAL GAEVRWASCN IFSTQDHAAA AIAAAGIPVF AFKGESLDEY WEFSHKIFEW 

       130        140        150        160        170        180 
PEGQPANMIL DDGGDATLLL MLGSKAEKDI GVIAHPTNEE ETALFASIKR HLAIDPHWYS 

       190        200        210        220        230        240 
KRLEHIQGVT EETTTGVHRL YQLEKDGHLP FPAINVNDSV TKSKFDNLYG CRESLVDGIK 

       250        260        270        280        290        300 
RATDVMVAGK VAVVLGYGDV GKGCAQSLRG LGATVWVTEI DPICALQAAM EGYRVVRMDE 

       310        320        330        340        350        360 
VADQADIFVT ATGNVGVITH EHMKKMRNNA IICNIGHFDS EIEVASLRQY QWENIKPQVD 

       370        380        390        400        410        420 
HIIFPDGKRV ILLAEGRLVN LGCATGHPSF VMSNSFTNQV LAQIELFANG HKYEKKVYVL 

       430        440        450        460 
PKHLDEKVAR LHLARIGARL TELSDQQAAY ISVPKQGPYK PDHYRY

« Hide

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ58639.1.
RefSeqNP_900635.1.

3D structure databases

SMRQ7NZF7. Positions 6-466.
ModBaseSearch...

Genome annotation databases

GeneID2550940.
GenomeReviewsGene locus CV_0965 in contig AE016825_GR.
KEGGcvi:CV_0965.
NMPDRfig|243365.1.peg.965.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMAVITHDHM.
PhylomeDBQ7NZF7.

Enzyme and pathway databases

BioCycCVIO243365:CV_0965-MONOMER.
BRENDA3.3.1.1. 415.

Family and domain databases

HAMAPMF_00563_B. AdoHcyase_B.
[Tree]
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...

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Entry information

Entry nameSAHH_CHRVO
AccessionPrimary (citable) accession number: Q7NZF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: February 9, 2010
This is version 51 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)

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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