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O67240 (SAHH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. 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:sahH
Ordered Locus Names:aq_1180
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length418 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
Reference 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 – 418418Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116941

Regions

Nucleotide binding151 – 1533NAD By similarity
Nucleotide binding214 – 2196NAD By similarity
Nucleotide binding293 – 2953NAD By similarity

Sites

Binding site531Substrate By similarity
Binding site1251Substrate By similarity
Binding site1501Substrate By similarity
Binding site1801Substrate By similarity
Binding site1841Substrate By similarity
Binding site1851NAD By similarity
Binding site2371NAD By similarity
Binding site2721NAD By similarity
Binding site3401NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
O67240 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0E778869976E7DA9

FASTA41846,840
        10         20         30         40         50         60 
MEFDVKDLSL AEEGLKRIEW AEMDMPVLRQ IRERFSKEKP LKGKKISACL HVTTETANLM 

        70         80         90        100        110        120 
RTLKEGGAEV YLTASNPLST QDDVAAALVK YFEIPVFAIR GEDRETYYKH LRAVIEKEPD 

       130        140        150        160        170        180 
VVIDDGADLI STLHKEYPGL AEKVLGGMEE TTTGVIRLRA MAEQGVLKFP IIAVNDAYTK 

       190        200        210        220        230        240 
HMFDNRYGTG QSTIDGILRA TNRLLAGSYF VVAGYGWCGK GVAQRARGMG AIVIVTEVDP 

       250        260        270        280        290        300 
IKALEARMDG FLVMPMEEAA KLGDFFVTVT GNIHVIRREH FEVMKDGAIV ANSGHFNVEI 

       310        320        330        340        350        360 
DIPALEEMAV EKREIRKEVT EYKLKDGRRI YLLAEGRLVN LAAAEGHPAS VMDMSFSNQA 

       370        380        390        400        410 
LSAEYIVKHH KELEKKVYRV PREIDEAVAR LKLNALGIKI DELTEEQKKY LSSWEMGT

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07197.1.
PIRE70401.
RefSeqNP_213804.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67240.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192586.
GenomeReviewsGene locus aq_1180 in contig AE000657_GR.
KEGGaae:aq_1180.
NMPDRfig|224324.1.peg.819.
PATRIC20959594. VBIAquAeo85532_0917.

Phylogenomic databases

HOGENOMHBG352029.
OMAVCNAGHF.
PhylomeDBO67240.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1180-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_AQUAE
AccessionPrimary (citable) accession number: O67240
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 80 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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