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Q2YQX8 (SAHH_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:BAB1_2099
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length466 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 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 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 – 466466Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024711

Regions

Nucleotide binding193 – 1953NAD By similarity
Nucleotide binding256 – 2616NAD By similarity
Nucleotide binding335 – 3373NAD By similarity

Sites

Binding site571Substrate By similarity
Binding site1321Substrate By similarity
Binding site1921Substrate By similarity
Binding site2221Substrate By similarity
Binding site2261Substrate By similarity
Binding site2271NAD By similarity
Binding site2791NAD By similarity
Binding site3141NAD By similarity
Binding site3801NAD By similarity

Secondary structure

1 .................................................................................. 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2YQX8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 6AB3B4B1C2F0BE41

FASTA46650,791
        10         20         30         40         50         60 
MTASQDFVVK DISLADWGRK ELDIAETEMP GLMAAREEFG KSQPLKGARI SGSLHMTIQT 

        70         80         90        100        110        120 
AVLIETLKVL GAEVRWASCN IFSTQDHAAA AIAATGTPVF AVKGETLEEY WTYTDQIFQW 

       130        140        150        160        170        180 
PDGEPSNMIL DDGGDATMYI LIGARAEAGE DVLSNPQSEE EEVLFAQIKK RMAATPGFFT 

       190        200        210        220        230        240 
KQRAAIKGVT EETTTGVNRL YQLQKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGIR 

       250        260        270        280        290        300 
RGTDVMMAGK VAVVCGYGDV GKGSAQSLAG AGARVKVTEV DPICALQAAM DGFEVVTLDD 

       310        320        330        340        350        360 
AASTADIVVT TTGNKDVITI DHMRKMKDMC IVGNIGHFDN EIQVAALRNL KWTNVKPQVD 

       370        380        390        400        410        420 
LIEFPDGKRL ILLSEGRLLN LGNATGHPSF VMSASFTNQV LGQIELFTRT DAYKNEVYVL 

       430        440        450        460 
PKHLDEKVAR LHLDKLGAKL TVLSEEQAAY IGVTPQGPFK SEHYRY

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM040264 Genomic DNA. Translation: CAJ12055.1.
RefSeqYP_415424.1. NC_007618.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N58X-ray2.39A/B/C/D8-466[»]
ProteinModelPortalQ2YQX8.
SMRQ2YQX8. Positions 5-466.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2YQX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3788612.
GenomeReviewsGene locus BAB1_2099 in contig AM040264_GR.
KEGGbmf:BAB1_2099.
PATRIC17847299. VBIBruMel86222_2185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBMEL359391:BAB1_2099-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_BRUA2
AccessionPrimary (citable) accession number: Q2YQX8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

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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