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Q3JY79 (SAHH_BURP1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BURPS1710b_0057
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]
Taxonomic identifier320372 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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 term3D-structure
Complete 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 – 473473Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024718

Regions

Nucleotide binding200 – 2023NAD By similarity
Nucleotide binding263 – 2686NAD By similarity
Nucleotide binding266 – 2672NAD HAMAP MF_00563
Nucleotide binding342 – 3443NAD By similarity
Nucleotide binding342 – 3432NAD HAMAP MF_00563

Sites

Binding site641Substrate
Binding site1391Substrate
Binding site1991Substrate
Binding site2291Substrate
Binding site2331Substrate
Binding site2341NAD By similarity
Binding site2861NAD
Binding site3211NAD
Binding site3871NAD

Secondary structure

1 ...................................................................................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3JY79 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 7A40ECDD0A47B596

FASTA47352,201
        10         20         30         40         50         60 
MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS 

        70         80         90        100        110        120 
LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF 

       130        140        150        160        170        180 
SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI ARPTNEEEVA LFKSIERHLE 

       190        200        210        220        230        240 
IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE 

       250        260        270        280        290        300 
SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY 

       310        320        330        340        350        360 
RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE 

       370        380        390        400        410        420 
NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY 

       430        440        450        460        470 
ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV SKAGPFKPDH YRY

« Hide

References

« Hide 'large scale' references
[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1710b.
[2]"Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei."
Seattle structural genomics center for infectious disease (SSGCID)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD.
[3]"Crystal structure of s-adenosyl-l-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furanosyl-adenine."
Joint center for structural genomics (JCSG)
Submitted (MAR-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000124 Genomic DNA. Translation: ABA47924.1.
RefSeqYP_331474.1. NC_007434.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D64X-ray2.30A/B1-473[»]
3GLQX-ray2.30A/B1-473[»]
ProteinModelPortalQ3JY79.
SMRQ3JY79. Positions 12-473.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JY79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3691538.
GenomeReviewsGene locus BURPS1710b_0057 in contig CP000124_GR.
KEGGbpm:BURPS1710b_0057.
PATRIC19232326. VBIBurPse115837_0057.
TIGRBURPS1710b_0057.

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ3JY79.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBPSE320372:BURPS1710B_A0064-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_BURP1
AccessionPrimary (citable) accession number: Q3JY79
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 54 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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