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Reviewed, UniProtKB/Swiss-Prot Q57AG3 (SAHH_BRUAB)

Last modified February 9, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BruAb1_2072
OrganismBrucella abortus [Complete proteome] [HAMAP]
Taxonomic identifier235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
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. 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: 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 – 466466Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024712

Regions

Region219 – 384166NAD binding By similarity

Sites

Binding site571Substrate By similarity
Binding site1321Substrate By similarity
Binding site1921Substrate By similarity
Binding site2221Substrate By similarity
Binding site2261Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57AG3-1 [UniParc].

Last modified May 10, 2005. 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]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX75371.1.
RefSeqYP_222732.1.

3D structure databases

HSSPHSSP built from PDB template 1B3R based on UniProtKB P10760.
SMRQ57AG3. Positions 5-466.
ModBaseSearch...

Genome annotation databases

GeneID3340511.
GenomeReviewsGene locus BruAb1_2072 in contig AE017223_GR.
KEGGbmb:BruAb1_2072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMAVITHDHM.
PhylomeDBQ57AG3.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_2072-MONOMER.
BRENDA3.3.1.1. 575.

Family and domain databases

HAMAPMF_00563_B. AdoHcyase_B.
[Tree]
InterProIPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
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]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSAHH_BRUAB
AccessionPrimary (citable) accession number: Q57AG3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 10, 2005
Last modified: February 9, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

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