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A1WXM7 (SAHH_HALHL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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
Ordered Locus Names:Hhal_1675
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Halorhodospira

Protein attributes

Sequence length430 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 – 430430Adenosylhomocysteinase HAMAP MF_00563
PRO_1000061125

Regions

Nucleotide binding157 – 1593NAD By similarity
Nucleotide binding220 – 2256NAD By similarity
Nucleotide binding299 – 3013NAD By similarity

Sites

Binding site561Substrate By similarity
Binding site1311Substrate By similarity
Binding site1561Substrate By similarity
Binding site1861Substrate By similarity
Binding site1901Substrate By similarity
Binding site1911NAD By similarity
Binding site2431NAD By similarity
Binding site2781NAD By similarity
Binding site3441NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WXM7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 1B0D75461642D506

FASTA43047,510
        10         20         30         40         50         60 
MSNQDYKVAD ISLADWGRKE IKIAESEMPG LMETRREFAA QKPLKGARIA GCLHMTIQTA 

        70         80         90        100        110        120 
VLIETLQELG AEVRWSSCNI FSTQDQAAAA VAANGTPVFA WKGETEEEYW WCIEQTINGP 

       130        140        150        160        170        180 
DGWKPNMLLD DGGDLTAVIH EQYPDMMKDI YGVSEETTTG VHRLYEMSRK GELGMPAFNV 

       190        200        210        220        230        240 
NDSVTKSKFD NLYGCRESLV DSIKRATDVM IAGKVAVVAG FGDVGKGSAQ SLRGLGAQVW 

       250        260        270        280        290        300 
VTEVDPICAL QASMDGYKVV TMEEAAPVAD IFVTATGNYN VITHDHMKAM KDEAIVCNIG 

       310        320        330        340        350        360 
HFDNEIDVAS LKQYKWDEIK PQVDHVEFPD GKKITLLAEG RLVNLGCATG HPSFVMSNSF 

       370        380        390        400        410        420 
TNQVMAQMEL YNNPGKYEKD VYVLPKHLDE KVAALHLGRV GANLTRLSEE QAGYIGVSVD 

       430 
GPFKPEWYRY

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000544 Genomic DNA. Translation: ABM62439.1.
RefSeqYP_001003241.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WXM7.
SMRA1WXM7. Positions 4-430.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1WXM7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4709919.
GenomeReviewsGene locus Hhal_1675 in contig CP000544_GR.
KEGGhha:Hhal_1675.
PATRIC22097627. VBIHalHal112047_1647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBA1WXM7.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycHHAL349124:HHAL_1675-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_HALHL
AccessionPrimary (citable) accession number: A1WXM7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 42 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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