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A4QC87 (SAHH_CORGB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:cgR_0861
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length478 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 – 478478Adenosylhomocysteinase HAMAP MF_00563
PRO_1000061124

Regions

Nucleotide binding202 – 2043NAD By similarity
Nucleotide binding265 – 2706NAD By similarity
Nucleotide binding344 – 3463NAD By similarity

Sites

Binding site571Substrate By similarity
Binding site1391Substrate By similarity
Binding site2011Substrate By similarity
Binding site2311Substrate By similarity
Binding site2351Substrate By similarity
Binding site2361NAD By similarity
Binding site2881NAD By similarity
Binding site3231NAD By similarity
Binding site3921NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A4QC87 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: C039C9248CF12820

FASTA47852,425
        10         20         30         40         50         60 
MAQVMDFKVA DLSLAEAGRH QIRLAEYEMP GLMQLRKEFA DEQPLKGARI AGSIHMTVQT 

        70         80         90        100        110        120 
AVLIETLTAL GAEVRWASCN IFSTQDEAAA AIVVGSGTVE EPAGVPVFAW KGESLEEYWW 

       130        140        150        160        170        180 
CINQIFSWGD ELPNMILDDG GDATMAVIRG REYEQAGLVP PAEANDSDEY IAFLGMLREV 

       190        200        210        220        230        240 
LAAEPGKWGK IAEAVKGVTE ETTTGVHRLY HFAEEGVLPF PAMNVNDAVT KSKFDNKYGT 

       250        260        270        280        290        300 
RHSLIDGINR ATDMLMGGKN VLVCGYGDVG KGCAEAFDGQ GARVKVTEAD PINALQALMD 

       310        320        330        340        350        360 
GYSVVTVDEA IEDADIVITA TGNKDIISFE QMLKMKDHAL LGNIGHFDNE IDMHSLLHRD 

       370        380        390        400        410        420 
DVTRTTIKPQ VDEFTFSTGR SIIVLSEGRL LNLGNATGHP SFVMSNSFAD QTIAQIELFQ 

       430        440        450        460        470 
NEGQYENEVY RLPKVLDEKV ARIHVEALGG QLTELTKEQA EYIGVDVAGP FKPEHYRY

« Hide

References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009044 Genomic DNA. Translation: BAF53834.1.
RefSeqYP_001137736.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QC87.
SMRA4QC87. Positions 6-478.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4QC87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4991882.
GenomeReviewsGene locus cgR_0861 in contig AP009044_GR.
KEGGcgt:cgR_0861.
PATRIC21506241. VBICorGlu58097_0894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

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_CORGB
AccessionPrimary (citable) accession number: A4QC87
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 40 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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