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A3MQW7 (SAHH_BURM7) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BMA10247_3134
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length473 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 – 473473Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024714

Regions

Nucleotide binding200 – 2023NAD By similarity
Nucleotide binding263 – 2686NAD By similarity
Nucleotide binding342 – 3443NAD By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A3MQW7 [UniParc].

Last modified April 3, 2007. 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

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000548 Genomic DNA. Translation: ABO05463.1.
RefSeqYP_001082653.1. NC_009080.1.

3D structure databases

ProteinModelPortalA3MQW7.
SMRA3MQW7. Positions 12-473.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MQW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4894372.
GenomeReviewsGene locus BMA10247_3134 in contig CP000548_GR.
KEGGbmn:BMA10247_3134.
PATRIC19148597. VBIBurMal96640_5328.
TIGRBMA10247_3134.

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBMAL320389:BMA10247_3134-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_BURM7
AccessionPrimary (citable) accession number: A3MQW7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 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