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Reviewed, UniProtKB/Swiss-Prot Q9YEF2 (SAHH_AERPE)

Last modified November 3, 2009. Version 59. 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: APE_0624.1
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length416 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; L-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 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 – 416416Adenosylhomocysteinase HAMAP MF_00563
PRO_0000117000

Regions

Region178 – 345168NAD binding By similarity

Sites

Binding site551Substrate By similarity
Binding site1261Substrate By similarity
Binding site1511Substrate By similarity
Binding site1811Substrate By similarity
Binding site1851Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YEF2-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: E145E95F5DDE9880

FASTA41645,919
        10         20         30         40         50         60 
MAQGFKVRDL SLAGEGRMQI EWAERHMPVL MRLRSSMGGD KPLSGVRVAA CLHVTKETAV 

        70         80         90        100        110        120 
LVETLRKWGA EVYLAPSNPL STQDEVAAAL AEAGIGVFAW RGMTPEEYKW ALSTVAGREP 

       130        140        150        160        170        180 
DIVIDDGADL HVLLHEEMRS VGEKVWGGTE ETTTGVIRLR ALEREGRLLY PVIAVNDALT 

       190        200        210        220        230        240 
KFMFDNRYGT GQSTVDGVLR ATNILIAGKT VVVAGYGWVG RGIAARFRGM GAKVVVTEVD 

       250        260        270        280        290        300 
PVRALEAAMD GFTVTTMDEA ASLGDVFITA TGNINVIDAR HMEKMKDGAI LANAGHFNVE 

       310        320        330        340        350        360 
INVAALEEMS VSKRRVRRYL DEYRLPDGRR LYLIGEGRLV NLVAAEGHPS EVMDMSFSNQ 

       370        380        390        400        410 
ALAVLKIAGE RGRLEKRVHR VERIQDEMVA RLKLETMGVR IDSLTEEQKL YLQKWK 

« Hide

References

[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K1.

Cross-references

Sequence databases

BA000002 Genomic DNA. Translation: BAA79594.2.
PIRB72649.
RefSeqNP_147374.2.

3D structure databases

HSSPHSSP built from PDB template 1LI4 based on UniProtKB P23526.
ModBaseSearch...

Genome annotation databases

GeneID1444774.
GenomeReviewsGene locus APE_0624.1 in contig BA000002_GR.
KEGGape:APE_0624.1.
NMPDRfig|272557.1.peg.482.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9YEF2.
OMAIRLKAMA.

Enzyme and pathway databases

BRENDA3.3.1.1. 256344.

Family and domain databases

HAMAPMF_00563.
[Tree]
InterProIPR015878. Ado_hCys_hydrolase_NAD-bd.
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...

Entry information

Entry nameSAHH_AERPE
AccessionPrimary (citable) accession number: Q9YEF2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: November 3, 2009
This is version 59 of the entry and version 2 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