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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)DescriptionActionsGraphical viewLength
Binding sitei56Substrate1
Sitei59Important for nucleoside inhibitor binding1
Binding sitei134Substrate1
Binding sitei200Substrate1
Binding sitei230Substrate1
Binding sitei234Substrate1
Binding sitei235NAD1 Publication1
Binding sitei287NAD1 Publication1
Binding sitei322NAD1 Publication1
Binding sitei391NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi201 – 203NAD1 Publication3
Nucleotide bindingi264 – 269NAD1 Publication6
Nucleotide bindingi343 – 345NAD1 Publication3

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)DescriptionActionsGraphical viewLength
Mutagenesisi59C → T: Decreases sensitivity towards inhibitors. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6076.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001169171 – 479AdenosylhomocysteinaseAdd BLAST479

PTM databases

SwissPalmiP50250.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi1208339. 9 interactors.
IntActiP50250. 9 interactors.
MINTiMINT-1556611.

Chemistry databases

BindingDBiP50250.

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Helixi14 – 24Combined sources11
Helixi25 – 27Combined sources3
Helixi29 – 37Combined sources9
Turni39 – 41Combined sources3
Turni43 – 46Combined sources4
Beta strandi48 – 53Combined sources6
Helixi57 – 68Combined sources12
Beta strandi72 – 76Combined sources5
Beta strandi78 – 81Combined sources4
Helixi85 – 91Combined sources7
Beta strandi97 – 100Combined sources4
Helixi107 – 118Combined sources12
Beta strandi121 – 125Combined sources5
Beta strandi129 – 136Combined sources8
Helixi137 – 155Combined sources19
Helixi161 – 163Combined sources3
Helixi167 – 180Combined sources14
Helixi186 – 191Combined sources6
Beta strandi196 – 199Combined sources4
Helixi202 – 213Combined sources12
Beta strandi219 – 223Combined sources5
Helixi228 – 231Combined sources4
Helixi234 – 251Combined sources18
Beta strandi258 – 263Combined sources6
Helixi267 – 279Combined sources13
Beta strandi282 – 286Combined sources5
Helixi290 – 297Combined sources8
Turni298 – 300Combined sources3
Helixi306 – 309Combined sources4
Turni310 – 312Combined sources3
Beta strandi314 – 318Combined sources5
Beta strandi321 – 326Combined sources6
Helixi328 – 331Combined sources4
Beta strandi339 – 342Combined sources4
Turni346 – 348Combined sources3
Helixi352 – 356Combined sources5
Beta strandi362 – 367Combined sources6
Beta strandi370 – 374Combined sources5
Beta strandi380 – 384Combined sources5
Helixi385 – 387Combined sources3
Helixi390 – 393Combined sources4
Helixi400 – 419Combined sources20
Turni420 – 422Combined sources3
Beta strandi423 – 425Combined sources3
Beta strandi428 – 431Combined sources4
Helixi435 – 446Combined sources12
Helixi447 – 449Combined sources3
Helixi458 – 464Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP50250.

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

HOGENOMiHOG000227986.
InParanoidiP50250.
KOiK01251.
OMAiEEYQWCL.
PhylomeDBiP50250.

Family and domain databases

CDDicd00401. SAHH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti243 – 244LP → YT in AAA21391 (PubMed:8206944).Curated2

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

EnsemblProtistsiCAD51574; CAD51574; PF3D7_0520900.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V8BX-ray2.40A/B/C/D1-479[»]
ProteinModelPortaliP50250.
SMRiP50250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1208339. 9 interactors.
IntActiP50250. 9 interactors.
MINTiMINT-1556611.

Chemistry databases

BindingDBiP50250.
ChEMBLiCHEMBL6076.

PTM databases

SwissPalmiP50250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiCAD51574; CAD51574; PF3D7_0520900.
GeneDBiPF3D7_0520900.1:pep.
GeneIDi813025.
KEGGipfa:PFE1050w.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_0520900.

Phylogenomic databases

HOGENOMiHOG000227986.
InParanoidiP50250.
KOiK01251.
OMAiEEYQWCL.
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

CDDicd00401. SAHH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase. 1 hit.
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...

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: November 30, 2016
This is version 116 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.