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B6J3R0 (SAHH_COXB2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:CbuG_2041
OrganismCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP]
Taxonomic identifier434923 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length438 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 – 438438Adenosylhomocysteinase HAMAP MF_00563
PRO_1000129278

Regions

Nucleotide binding165 – 1673NAD By similarity
Nucleotide binding228 – 2336NAD By similarity
Nucleotide binding307 – 3093NAD By similarity

Sites

Binding site641Substrate By similarity
Binding site1391Substrate By similarity
Binding site1641Substrate By similarity
Binding site1941Substrate By similarity
Binding site1981Substrate By similarity
Binding site1991NAD By similarity
Binding site2511NAD By similarity
Binding site2861NAD By similarity
Binding site3521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J3R0 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: EF9BC88F62DA390F

FASTA43848,868
        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 ARLHLERVGG 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].
Strain: CbuG_Q212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001019 Genomic DNA. Translation: ACJ19282.1.
RefSeqYP_002304427.1. NC_011527.1.

3D structure databases

ProteinModelPortalB6J3R0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6J3R0.

Proteomic databases

PRIDEB6J3R0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7014457.
GenomeReviewsGene locus CbuG_2041 in contig CP001019_GR.
KEGGcbg:CbuG_2041.
PATRIC17915208. VBICoxBur10955_2043.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

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_COXB2
AccessionPrimary (citable) accession number: B6J3R0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 28 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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