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Reviewed, UniProtKB/Swiss-Prot Q8YX05 (SAHH_ANASP)

Last modified November 3, 2009. Version 50. 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: alr1414
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length425 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 – 425425Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116940

Regions

Region184 – 351168NAD binding By similarity

Sites

Binding site601Substrate By similarity
Binding site1321Substrate By similarity
Binding site1571Substrate By similarity
Binding site1871Substrate By similarity
Binding site1911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YX05-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 38B232B91E0E46E2

FASTA42546,172
        10         20         30         40         50         60 
MTATSPRLKH EVKDLALAPL GRQRIEWAGR EMPVLRQIRD RFAQEKPFAG LRLVACAHIT 

        70         80         90        100        110        120 
TETAHLAIAL KAGGADAVLI ASNPLSTQDD VAASLVLDHE IPVFAQKGED NATYNRHVQI 

       130        140        150        160        170        180 
ALDHRPNIII DDGSDVVATL VQERQHQIAD LIGTTEETTT GIVRLRAMFK DGVLTFPAVN 

       190        200        210        220        230        240 
VNDADTKHFF DNRYGTGQST LDGIIRATNI LLAGKNVVVV GYGWCGKGTA LRARGMGANV 

       250        260        270        280        290        300 
IVTEIDPIKA IEAVMDGFRV LPMAEAAPQG DIFITVTGNK HVVRGEHFDV MKDGAIVCNS 

       310        320        330        340        350        360 
GHFDLELDLK YLAANAKEIK EVRPFTEEYK LTNGKSVVVL GQGRLINLAA AEGHPSAVMD 

       370        380        390        400        410        420 
MSFANQALAC EYLVKNKGKL APGLHSIPVE VDQEIARLKL QAMGIYIDSL TPEQIEYINS 


WTSGT 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000019 Genomic DNA. Translation: BAB73371.1.
PIRAC1983.
RefSeqNP_485457.1.

3D structure databases

HSSPHSSP built from PDB template 1K0U based on UniProtKB P10760.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YX05.

Genome annotation databases

GeneID1105009.
GenomeReviewsGene locus alr1414 in contig BA000019_GR.
KEGGana:alr1414.
NMPDRfig|103690.1.peg.1724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8YX05.
OMAIRLKAMA.

Enzyme and pathway databases

BioCycNSP103690:ALR1414-MON.

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_ANASP
AccessionPrimary (citable) accession number: Q8YX05
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: November 3, 2009
This is version 50 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)

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