Skip Header

Contribute Send feedback
Read comments (?) or add your own

P50250 (SAHH_PLAF7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1
Alternative name(s):
PfSAHH
S-adenosyl-L-homocysteine hydrolase
Gene names
ORF Names:PFE1050w
OrganismPlasmodium falciparum (isolate 3D7)
Taxonomic identifier36329 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit.

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Subunit structure

Homotetramer. Ref.5

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNAD
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Adenosylhomocysteinase
PRO_0000116917

Regions

Nucleotide binding201 – 2033NAD
Nucleotide binding264 – 2696NAD
Nucleotide binding343 – 3453NAD

Sites

Binding site561Substrate
Binding site1341Substrate
Binding site2001Substrate
Binding site2301Substrate
Binding site2341Substrate
Binding site2351NAD
Binding site2871NAD
Binding site3221NAD
Binding site3911NAD
Site591Important for nucleoside inhibitor binding

Experimental info

Mutagenesis591C → T: Decreases sensitivity towards inhibitors. Ref.5
Sequence conflict243 – 2442LP → YT in AAA21391. Ref.1

Secondary structure

1 .......................................................................................... 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50250 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: CC420C381466EEEF

FASTA47953,839
        10         20         30         40         50         60 
MVENKSKVKD ISLAPFGKMQ MEISENEMPG LMRIREEYGK DQPLKNAKIT GCLHMTVECA 

        70         80         90        100        110        120 
LLIETLQKLG AQIRWCSCNI YSTADYAAAA VSTLENVTVF AWKNETLEEY WWCVESALTW 

       130        140        150        160        170        180 
GDGDDNGPDM IVDDGGDATL LVHKGVEYEK LYEEKNILPD PEKAKNEEER CFLTLLKNSI 

       190        200        210        220        230        240 
LKNPKKWTNI AKKIIGVSEE TTTGVLRLKK MDKQNELLFT AINVNDAVTK QKYDNVYGCR 

       250        260        270        280        290        300 
HSLPDGLMRA TDFLISGKIV VICGYGDVGK GCASSMKGLG ARVYITEIDP ICAIQAVMEG 

       310        320        330        340        350        360 
FNVVTLDEIV DKGDFFITCT GNVDVIKLEH LLKMKNNAVV GNIGHFDDEI QVNELFNYKG 

       370        380        390        400        410        420 
IHIENVKPQV DRITLPNGNK IIVLARGRLL NLGCATGHPA FVMSFSFCNQ TFAQLDLWQN 

       430        440        450        460        470 
KDTNKYENKV YLLPKHLDEK VALYHLKKLN ASLTELDDNQ CQFLGVNKSG PFKSNEYRY

« Hide

References

« Hide 'large scale' references
[1]"Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli."
Creedon K.A., Rathod P.K., Wellems T.E.
J. Biol. Chem. 269:16364-16370(1994) [PubMed: 8206944] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"S-adenosyl-L-homocysteine hydrolase from Plasmodium falciparum: structure, evolution, and interactions with inhibitors."
Bujnicki J.M., Prigge S.T., Caridha D., Chiang P.K.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genome sequence of the human malaria parasite Plasmodium falciparum."
Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S. expand/collapse author list , Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.
Nature 419:498-511(2002) [PubMed: 12368864] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[4]"Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."
Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D., Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K., Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T., Christodoulou Z. expand/collapse author list , Clark L., Clark R., Corton C., Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R., Sulston J.E., Craig A., Newbold C., Barrell B.G.
Nature 419:527-531(2002) [PubMed: 12368867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[5]"Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum."
Tanaka N., Nakanishi M., Kusakabe Y., Shiraiwa K., Yabe S., Ito Y., Kitade Y., Nakamura K.T.
J. Mol. Biol. 343:1007-1017(2004) [PubMed: 15476817] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND ADENOSINE, SUBUNIT, MUTAGENESIS OF CYS-59.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U07365 mRNA. Translation: AAA21391.1.
AF525293 Genomic DNA. Translation: AAM90981.1.
AL844504 Genomic DNA. Translation: CAD51574.1.
PIRA54040.
RefSeqXP_001351767.1. XM_001351731.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8BX-ray2.40A/B/C/D1-479[»]
ProteinModelPortalP50250.
SMRP50250. Positions 4-479.
ModBaseSearch...

Protein-protein interaction databases

IntActP50250. 9 interactions.
MINTMINT-1556611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPFE1050w:mRNA; PFE1050w:pep; PFE1050w.
GeneID813025.
KEGGpfa:PFE1050w.
NMPDRfig|36329.1.peg.3240.

Organism-specific databases

EuPathDBEupathDB:PFE1050w.

Phylogenomic databases

GeneTreeEPrGT00050000005670.
HOGENOMHBG352029.
OMAELFTKTE.
ProtClustDBPTZ00075.

Family and domain databases

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_PLAF7
AccessionPrimary (citable) accession number: P50250
Secondary accession number(s): Q7K6A6, Q8MUG1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents