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Reviewed, UniProtKB/Swiss-Prot A9KD88 (SAHH_COXBN)

Last modified September 22, 2009. Version 19. 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: CBUD_2132
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length438 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 – 438438Adenosylhomocysteinase HAMAP MF_00563
PRO_1000129279

Regions

Region191 – 356166NAD binding By similarity

Sites

Binding site641Substrate By similarity
Binding site1391Substrate By similarity
Binding site1641Substrate By similarity
Binding site1941Substrate By similarity
Binding site1981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KD88-1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: EF9BC88F64BA5F0F

FASTA43848,882
        10         20         30         40         50         60 
MENDMETATM TQDYHIANIN LADWGRKEIE IAETEMPGLM ALRKKYKNAK PLKGARIAGC 

        70         80         90        100        110        120 
IHMTIQTAVL IETLMLLGAE VRWSSCNIFS TQDHAAAALA QKGIPIFAWK GETEEEYWRC 

       130        140        150        160        170        180 
IASTLEGPKG WTPNLLLDDG GDLTAHTLQK HPELCQNIRG VSEETTTGVH RLYRMLKEGS 

       190        200        210        220        230        240 
LKFPAINVND SVTKSKFDNL YGCRESLIDS IKRATDVMIA GKRVVVCGYG DVGKGCAQSL 

       250        260        270        280        290        300 
RAYGATVYIT EIDPICALQA AMEGYRVVTM DEMADSADIF VTATGNTDII THEHMLKMKD 

       310        320        330        340        350        360 
QAIVCNIGHF DNEIDIASLQ DYQWMNIKPQ VDQVIFPDGK RLTVLAQGRL VNLGCATGHP 

       370        380        390        400        410        420 
SFVMSNSFTN QVLAQIELWQ YPEKYPIGVY VLPKHLDEEV ARLHLERVGA KLTTLTEKQA 

       430 
DYIGVDPEGP FKSEHYRY 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed: 19047403] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000733 Genomic DNA. Translation: ABS76996.2.
RefSeqYP_001425436.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5458160.
GenomeReviewsGene locus CBUD_2132 in contig CP000733_GR.
KEGGcbd:CBUD_2132.

Organism-specific databases

CMRSearch...

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]
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSAHH_COXBN
AccessionPrimary (citable) accession number: A9KD88
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: September 22, 2009
This is version 19 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