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Reviewed, UniProtKB/Swiss-Prot Q8FRJ4 (SAHH_COREF)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: CE0767
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 478478Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116959

Regions

Region228 – 396169NAD binding By similarity

Sites

Binding site571Substrate By similarity
Binding site1391Substrate By similarity
Binding site2011Substrate By similarity
Binding site2311Substrate By similarity
Binding site2351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FRJ4-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A75845A1A3F3A978

FASTA47852,777
        10         20         30         40         50         60 
MAKVTDFKVA DLSLAEAGRH QIRLAEYEMP GLMQLRREYA EEQPLKGARI AGSIHMTVQT 

        70         80         90        100        110        120 
AVLIETLTAL GAEVRWASCN IFSTQDEAAA AIVVGDGTPE DPQGVPVFAW KGETLDEYWW 

       130        140        150        160        170        180 
CINQIFSWEG ELPNMILDDG GDATMAVIRG REYEKAGVVP QPEANDSDEY IAFLGMLREV 

       190        200        210        220        230        240 
LAEEPDKWTR LADSIKGVTE ETTTGVHRLY HFAEEGVLPF PAMNVNDAVT KSKFDNKYGT 

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

       310        320        330        340        350        360 
GYSVVTVDEA IADADIVITA TGNKDIISYE QMLKMKDHAL LGNIGHFDNE IDMHSLLHRD 

       370        380        390        400        410        420 
DVIRTTIKPQ VDEFTFPNGK SIIVLSEGRL LNLGNATGHP SFVMSTSFAD QTIAQIELFQ 

       430        440        450        460        470 
NEGQYENQVY RLPKILDEKV ARIHVEALGG KLTELTKEQA EYIGVDVAGP FKPEHYRY 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

BA000035 Genomic DNA. Translation: BAC17577.1.
RefSeqNP_737377.1.

3D structure databases

HSSPHSSP built from PDB template 1B3R based on UniProtKB P10760.
ModBaseSearch...

Genome annotation databases

GeneID1032872.
GenomeReviewsGene locus CE0767 in contig BA000035_GR.
KEGGcef:CE0767.
NMPDRfig|196164.1.peg.767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FRJ4.
OMAHMRAMKD.

Enzyme and pathway databases

BioCycCEFF196164:CE0767-MON.
BRENDA3.3.1.1. 277326.

Family and domain databases

HAMAPMF_00563.
[Tree]
InterProIPR015878. Ado_hCys_hydrolase_NAD-bd.
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_COREF
AccessionPrimary (citable) accession number: Q8FRJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 44 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

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