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Protein

Adenosylhomocysteinase

Gene

PFE1050w

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

NAD+Note: Binds 1 NAD+ per subunit.

Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (PFE1050w)
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Sitei59 – 591Important for nucleoside inhibitor binding
Binding sitei134 – 1341Substrate
Binding sitei200 – 2001Substrate
Binding sitei230 – 2301Substrate
Binding sitei234 – 2341Substrate
Binding sitei235 – 2351NAD1 Publication
Binding sitei287 – 2871NAD1 Publication
Binding sitei322 – 3221NAD1 Publication
Binding sitei391 – 3911NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2033NAD1 Publication
Nucleotide bindingi264 – 2696NAD1 Publication
Nucleotide bindingi343 – 3453NAD1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi3.3.1.1. 4889.
ReactomeiR-PFA-156581. Methylation.
R-PFA-1614635. Sulfur amino acid metabolism.
UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylhomocysteinase (EC:3.3.1.1)
Short name:
AdoHcyase
Alternative name(s):
PfSAHH
S-adenosyl-L-homocysteine hydrolase
Gene namesi
ORF Names:PFE1050w
OrganismiPlasmodium falciparum (isolate 3D7)
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000001450 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_0520900.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591C → T: Decreases sensitivity towards inhibitors. 1 Publication

Chemistry

ChEMBLiCHEMBL6076.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479AdenosylhomocysteinasePRO_0000116917Add
BLAST

PTM databases

SwissPalmiP50250.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi1208339. 9 interactions.
IntActiP50250. 9 interactions.
MINTiMINT-1556611.

Chemistry

BindingDBiP50250.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Helixi14 – 2411Combined sources
Helixi25 – 273Combined sources
Helixi29 – 379Combined sources
Turni39 – 413Combined sources
Turni43 – 464Combined sources
Beta strandi48 – 536Combined sources
Helixi57 – 6812Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 814Combined sources
Helixi85 – 917Combined sources
Beta strandi97 – 1004Combined sources
Helixi107 – 11812Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi129 – 1368Combined sources
Helixi137 – 15519Combined sources
Helixi161 – 1633Combined sources
Helixi167 – 18014Combined sources
Helixi186 – 1916Combined sources
Beta strandi196 – 1994Combined sources
Helixi202 – 21312Combined sources
Beta strandi219 – 2235Combined sources
Helixi228 – 2314Combined sources
Helixi234 – 25118Combined sources
Beta strandi258 – 2636Combined sources
Helixi267 – 27913Combined sources
Beta strandi282 – 2865Combined sources
Helixi290 – 2978Combined sources
Turni298 – 3003Combined sources
Helixi306 – 3094Combined sources
Turni310 – 3123Combined sources
Beta strandi314 – 3185Combined sources
Beta strandi321 – 3266Combined sources
Helixi328 – 3314Combined sources
Beta strandi339 – 3424Combined sources
Turni346 – 3483Combined sources
Helixi352 – 3565Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi370 – 3745Combined sources
Beta strandi380 – 3845Combined sources
Helixi385 – 3873Combined sources
Helixi390 – 3934Combined sources
Helixi400 – 41920Combined sources
Turni420 – 4223Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi428 – 4314Combined sources
Helixi435 – 44612Combined sources
Helixi447 – 4493Combined sources
Helixi458 – 4647Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8BX-ray2.40A/B/C/D1-479[»]
ProteinModelPortaliP50250.
SMRiP50250. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50250.

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

HOGENOMiHOG000227986.
InParanoidiP50250.
KOiK01251.
OMAiNLVHERF.
PhylomeDBiP50250.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 2 hits.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVENKSKVKD ISLAPFGKMQ MEISENEMPG LMRIREEYGK DQPLKNAKIT
60 70 80 90 100
GCLHMTVECA LLIETLQKLG AQIRWCSCNI YSTADYAAAA VSTLENVTVF
110 120 130 140 150
AWKNETLEEY WWCVESALTW GDGDDNGPDM IVDDGGDATL LVHKGVEYEK
160 170 180 190 200
LYEEKNILPD PEKAKNEEER CFLTLLKNSI LKNPKKWTNI AKKIIGVSEE
210 220 230 240 250
TTTGVLRLKK MDKQNELLFT AINVNDAVTK QKYDNVYGCR HSLPDGLMRA
260 270 280 290 300
TDFLISGKIV VICGYGDVGK GCASSMKGLG ARVYITEIDP ICAIQAVMEG
310 320 330 340 350
FNVVTLDEIV DKGDFFITCT GNVDVIKLEH LLKMKNNAVV GNIGHFDDEI
360 370 380 390 400
QVNELFNYKG IHIENVKPQV DRITLPNGNK IIVLARGRLL NLGCATGHPA
410 420 430 440 450
FVMSFSFCNQ TFAQLDLWQN KDTNKYENKV YLLPKHLDEK VALYHLKKLN
460 470
ASLTELDDNQ CQFLGVNKSG PFKSNEYRY
Length:479
Mass (Da):53,839
Last modified:October 25, 2005 - v2
Checksum:iCC420C381466EEEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2442LP → YT in AAA21391 (PubMed:8206944).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07365 mRNA. Translation: AAA21391.1.
AF525293 Genomic DNA. Translation: AAM90981.1.
AL844504 Genomic DNA. Translation: CAD51574.1.
PIRiA54040.
RefSeqiXP_001351767.1. XM_001351731.1.

Genome annotation databases

EnsemblProtistsiPFE1050w:mRNA; PFE1050w:pep; PFE1050w.
GeneDBiPF3D7_0520900.1:pep.
GeneIDi813025.
KEGGipfa:PFE1050w.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07365 mRNA. Translation: AAA21391.1.
AF525293 Genomic DNA. Translation: AAM90981.1.
AL844504 Genomic DNA. Translation: CAD51574.1.
PIRiA54040.
RefSeqiXP_001351767.1. XM_001351731.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8BX-ray2.40A/B/C/D1-479[»]
ProteinModelPortaliP50250.
SMRiP50250. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1208339. 9 interactions.
IntActiP50250. 9 interactions.
MINTiMINT-1556611.

Chemistry

BindingDBiP50250.
ChEMBLiCHEMBL6076.

PTM databases

SwissPalmiP50250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPFE1050w:mRNA; PFE1050w:pep; PFE1050w.
GeneDBiPF3D7_0520900.1:pep.
GeneIDi813025.
KEGGipfa:PFE1050w.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_0520900.

Phylogenomic databases

HOGENOMiHOG000227986.
InParanoidiP50250.
KOiK01251.
OMAiNLVHERF.
PhylomeDBiP50250.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.
BRENDAi3.3.1.1. 4889.
ReactomeiR-PFA-156581. Methylation.
R-PFA-1614635. Sulfur amino acid metabolism.

Miscellaneous databases

EvolutionaryTraceiP50250.
PROiP50250.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 2 hits.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. 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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND ADENOSINE, SUBUNIT, MUTAGENESIS OF CYS-59.

Entry informationi

Entry nameiSAHH_PLAF7
AccessioniPrimary (citable) accession number: P50250
Secondary accession number(s): Q7K6A6, Q8MUG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 25, 2005
Last modified: June 8, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.