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A0M5W6 (SAHH_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:GFO_3067
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length438 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 – 438438Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024727

Regions

Nucleotide binding163 – 1653NAD By similarity
Nucleotide binding226 – 2316NAD By similarity
Nucleotide binding305 – 3073NAD By similarity

Sites

Binding site611Substrate By similarity
Binding site1371Substrate By similarity
Binding site1621Substrate By similarity
Binding site1921Substrate By similarity
Binding site1961Substrate By similarity
Binding site1971NAD By similarity
Binding site2491NAD By similarity
Binding site2841NAD By similarity
Binding site3521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M5W6 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: ABB7A4B0C28EC1AF

FASTA43848,545
        10         20         30         40         50         60 
MSTKTVPYTA YKVKDIELAE YGRREIELAE AEMPGLMALR KEYGASKPLK GARIAGCLHM 

        70         80         90        100        110        120 
TIQTAVLIET LVELGANVTW SSCNIFSTQD HAAAAIAAAG IPVYAWKGLT EEEFNWCIEQ 

       130        140        150        160        170        180 
TLFFGEDRKP LNMILDDGGD LTNMVLDEYP ELAEGIKGLS EETTTGVHRL YERMKKGTLP 

       190        200        210        220        230        240 
MPAINVNDSV TKSKFDNKYG CRESAVDAIR RATDVMLAGK RVVVCGYGDV GKGTAQSFKG 

       250        260        270        280        290        300 
AGSIVTVTEI DPICALQAAM DGFEVKQLET VLPKADIVIT TTGNKDIVRP EHFEAMKDKT 

       310        320        330        340        350        360 
IVANIGHFDN EIAVSWLNEK HGDSKVEIKP QVDKYTINGK DIILLAEGRL VNLGCATGHP 

       370        380        390        400        410        420 
SFVMSNSFTN QTLAQIELWK NTDEYKNEVY MLPKHLDEKV AKLHLERIGV ELTELKQDQA 

       430 
EYIGVTVEGP YKPEYYRY 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL68011.1.
RefSeqYP_863078.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M5W6.
SMRA0M5W6. Positions 11-438.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M5W6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4651175.
GenomeReviewsGene locus GFO_3067 in contig CU207366_GR.
KEGGgfo:GFO_3067.
NMPDRfig|411154.5.peg.2888.
PATRIC22074874. VBIGraFor5527_2953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBA0M5W6.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycGFOR411154:GFO_3067-MONOMER.

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_GRAFK
AccessionPrimary (citable) accession number: A0M5W6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 45 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