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Q6G1D6 (SAHH_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:BQ00290
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length465 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 – 465465Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116945

Regions

Nucleotide binding192 – 1943NAD By similarity
Nucleotide binding255 – 2606NAD By similarity
Nucleotide binding334 – 3363NAD By similarity

Sites

Binding site561Substrate By similarity
Binding site1311Substrate By similarity
Binding site1911Substrate By similarity
Binding site2211Substrate By similarity
Binding site2251Substrate By similarity
Binding site2261NAD By similarity
Binding site2781NAD By similarity
Binding site3131NAD By similarity
Binding site3791NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G1D6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: CDD508B7C9A46AC6

FASTA46551,047
        10         20         30         40         50         60 
MAAQDYVVKD IALAAYGRKE IDIAETEMPG LMACREEFSF SQPLRGARIS GSLHITIQTA 

        70         80         90        100        110        120 
VLIETLKAIG ADVRWSSSNI FSTQDHAAAA IAATGTAVFG VKGETLEEYW AYIDAIFQWP 

       130        140        150        160        170        180 
DGNPSNLILD DGADATNYIL TGSRAEVNKD ILSYPKTKEE EFFFKQIQKR MKITPGFFTR 

       190        200        210        220        230        240 
QRTAIKGVSE ETTTGVLRLY QLQKEGLLPF PAINVNDSVT KSKFDNKYGC KESLVDGIRR 

       250        260        270        280        290        300 
GTDVMIAGKT AIVCGYGNVG KGSAASLSGA GARVKITEID PICALQAAMD GYEVVTLDDA 

       310        320        330        340        350        360 
ASSADIIITT TGNKDVVRLD HMRQVKDMCI LGNIGHFDNE IQVSALRNLP WTNIKPQVDI 

       370        380        390        400        410        420 
VTFPDGKRII LLSEGRLLNL GNATGHPSFV MSASFTNQVL AQIELFTRAE HYKNEVTVLP 

       430        440        450        460 
KRLDEKVARL HLDRLGVKLS VLSEEQAVYI GVTPQGPYKP NHYRY

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX897700 Genomic DNA. Translation: CAF25536.1.
RefSeqYP_031756.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G1D6.
SMRQ6G1D6. Positions 4-465.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2866636.
GenomeReviewsGene locus BQ00290 in contig BX897700_GR.
KEGGbqu:BQ00290.
NMPDRfig|283165.1.peg.26.
PATRIC31951183. VBIBarQui58630_0035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ6G1D6.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBQUI283165:BQ00290-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_BARQU
AccessionPrimary (citable) accession number: Q6G1D6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 53 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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