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Q18EV6 (SAHH_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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
Synonyms:achY
Ordered Locus Names:HQ3414A
OrganismHaloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloquadratum

Protein attributes

Sequence length432 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 – 432432Adenosylhomocysteinase HAMAP MF_00563
PRO_0000260219

Regions

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

Sites

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
Q18EV6 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: DB9BBA686AC2774A

FASTA43246,864
        10         20         30         40         50         60 
MSAYSPLSAQ LDADTDVDVE STRTEGRRKM EWTLQHMPIL QELRARFAET KPLAGETIGM 

        70         80         90        100        110        120 
AMHVEAKTAN LVELLALGGA EVAITGCNPL STHDDVSAAL DSNENVTSYA KRGVDEEAYY 

       130        140        150        160        170        180 
DAIEAVVAHE PTITIDDGMD MVYAIHEDHP DLLDTIIGGA EETTTGVHRL RAMDEDDELQ 

       190        200        210        220        230        240 
YPVFAVNDTP MKRLFDNVHG TGESALATIA MTTNLSYAGK NVVVAGYGYC GKGVAQKAAG 

       250        260        270        280        290        300 
QNANVIVTEV EPRRALEAHM EGYEVMPMNE AATRGDVFVT TTGNRDVITQ EDFEVMSDGA 

       310        320        330        340        350        360 
ILANAGHFDV EINLEELSEL AIDTYEARDG VQAYELGDGR RLNVLAEGRL VNLAAPIALG 

       370        380        390        400        410        420 
HPAEVMDQSF GIQAVCVREL IENKSSYDAG VHNVPDELDR EVAEIKLKAE GVDIDSLTQT 

       430 
QSEYLDSWSH GT

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180088 Genomic DNA. Translation: CAJ53511.1.
RefSeqYP_659099.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18EV6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ18EV6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4193683.
GenomeReviewsGene locus HQ3414A in contig AM180088_GR.
KEGGhwa:HQ3414A.
NMPDRfig|362976.6.peg.2416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04158.
HOGENOMHBG352029.
OMAEGDIFIT.
PhylomeDBQ18EV6.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycHWAL362976:HQ3414A-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_HALWD
AccessionPrimary (citable) accession number: Q18EV6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 25, 2006
Last modified: January 25, 2012
This is version 47 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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