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Q04NN6 (SAHH_LEPBJ) 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
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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:LBJ_4089
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length436 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 – 436436Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024729

Regions

Nucleotide binding162 – 1643NAD By similarity
Nucleotide binding225 – 2306NAD By similarity
Nucleotide binding304 – 3063NAD By similarity

Sites

Binding site621Substrate By similarity
Binding site1361Substrate By similarity
Binding site1611Substrate By similarity
Binding site1911Substrate By similarity
Binding site1951Substrate By similarity
Binding site1961NAD By similarity
Binding site2481NAD By similarity
Binding site2831NAD By similarity
Binding site3521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04NN6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F4BD8B927CAFC3E1

FASTA43648,096
        10         20         30         40         50         60 
MSATTQEKGL NYKVKDLSQA EWGRQEIILA EKEMPGLMAL RQEYKGKKPL AGARIAGSLH 

        70         80         90        100        110        120 
MTIQTAVLIE TLTELGAEVR WSSCNIFSTQ DHAAAAIAKA GVPVFAWKGE TEEEYWWCIE 

       130        140        150        160        170        180 
QTLFFGDKGP NMILDDGGDL TAYVHEKYPK LLSEIRGISE ETTTGVKSLY KLLKKGELKV 

       190        200        210        220        230        240 
PAFNVNDSVT KSKFDNLYGC RESLADGIKR ATDVMLAGKV ALVCGFGDVG KGSAASLRNF 

       250        260        270        280        290        300 
GARVIVTEID PICALQASME GYQVLRVEDI IEQVDIVVTA TGNDDIITLE HMKAMKDGAI 

       310        320        330        340        350        360 
LCNIGHFDTE IQMSRLNSEK GVTKKEIKPQ VDKYTFPDGK SIVVLAEGRL VNLGCATGHP 

       370        380        390        400        410        420 
SFVMSCSFTN QVLAQIELYN NKYELGVYTL PKHLDEKVAA LHLEQLGVRL TKLNQKQADY 

       430 
LGVPLNGPFK PENYRY

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000351 Genomic DNA. Translation: ABJ77484.1.
RefSeqYP_802242.1. NC_008511.1.

3D structure databases

ProteinModelPortalQ04NN6.
SMRQ04NN6. Positions 10-436.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ04NN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4412366.
GenomeReviewsGene locus LBJ_4089 in contig CP000351_GR.
KEGGlbj:LBJ_4089.
PATRIC22362601. VBILepBor13265_3983.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ04NN6.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycLBOR355277:LBJ_4089-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_LEPBJ
AccessionPrimary (citable) accession number: Q04NN6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
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

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