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Protein

Adenosylhomocysteinase

Gene

Ahcy

Organism
Mus musculus (Mouse)
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. Putative adenosylhomocysteinase 2 (Ahcyl1), Adenosylhomocysteinase, Adenosylhomocysteinase (Ahcyl2), Putative adenosylhomocysteinase 3 (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase, Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase, Adenosylhomocysteinase (Ahcyl2)
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 sitei57 – 571SubstrateBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Binding sitei190 – 1901SubstrateBy similarity

GO - Molecular functioni

  • adenosylhomocysteinase activity Source: MGI
  • copper ion binding Source: MGI
  • protein self-association Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-156581. Methylation.
R-MMU-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):
CUBP
Liver copper-binding protein
S-adenosyl-L-homocysteine hydrolase
Gene namesi
Name:Ahcy
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 16, Chromosome 2

Organism-specific databases

MGIiMGI:87968. Ahcy.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 432431AdenosylhomocysteinasePRO_0000116903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei193 – 1931PhosphotyrosineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP50247.
PaxDbiP50247.
PeptideAtlasiP50247.
PRIDEiP50247.

2D gel databases

REPRODUCTION-2DPAGEP50247.

PTM databases

iPTMnetiP50247.
PhosphoSiteiP50247.
SwissPalmiP50247.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027597.
CleanExiMM_AHCY.
ExpressionAtlasiP50247. baseline and differential.
GenevisibleiP50247. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Traf1P394283EBI-646982,EBI-520123

GO - Molecular functioni

  • protein self-association Source: MGI

Protein-protein interaction databases

IntActiP50247. 5 interactions.
MINTiMINT-1855506.
STRINGi10090.ENSMUSP00000127198.

Chemistry

BindingDBiP50247.

Structurei

3D structure databases

ProteinModelPortaliP50247.
SMRiP50247. Positions 3-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 350168NAD bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
InParanoidiP50247.
KOiK01251.
OMAiKSDQYAV.
OrthoDBiEOG091G06EB.
PhylomeDBiP50247.
TreeFamiTF300415.

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. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI
60 70 80 90 100
AGCLHMTVET AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF
110 120 130 140 150
AWKGETDEEY LWCIEQTLHF KDGPLNMILD DGGDLTNLIH TKYPQLLSGI
160 170 180 190 200
RGISEETTTG VHNLYKMMSN GILKVPAINV NDSVTKSKFD NLYGCRESLI
210 220 230 240 250
DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL
260 270 280 290 300
QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG
310 320 330 340 350
HFDVEIDVKW LNENAVEKVN IKPQVDRYWL KNGRRIILLA EGRLVNLGCA
360 370 380 390 400
MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG
410 420 430
KLNVKLTKLT EKQAQYLGMP INGPFKPDHY RY
Length:432
Mass (Da):47,688
Last modified:January 23, 2007 - v3
Checksum:i15CCD20B7088D5CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741K → N in AAA70378 (PubMed:7657650).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32836 mRNA. Translation: AAA70378.1.
BC015304 mRNA. Translation: AAH15304.1.
CCDSiCCDS16942.1.
RefSeqiNP_001291457.1. NM_001304528.1.
NP_057870.3. NM_016661.3.
UniGeneiMm.330692.
Mm.371964.

Genome annotation databases

EnsembliENSMUST00000054607; ENSMUSP00000061851; ENSMUSG00000027597.
ENSMUST00000059524; ENSMUSP00000127198; ENSMUSG00000048087.
GeneIDi11615.
269378.
KEGGimmu:11615.
mmu:269378.
UCSCiuc008nka.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32836 mRNA. Translation: AAA70378.1.
BC015304 mRNA. Translation: AAH15304.1.
CCDSiCCDS16942.1.
RefSeqiNP_001291457.1. NM_001304528.1.
NP_057870.3. NM_016661.3.
UniGeneiMm.330692.
Mm.371964.

3D structure databases

ProteinModelPortaliP50247.
SMRiP50247. Positions 3-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50247. 5 interactions.
MINTiMINT-1855506.
STRINGi10090.ENSMUSP00000127198.

Chemistry

BindingDBiP50247.
ChEMBLiCHEMBL2389.

PTM databases

iPTMnetiP50247.
PhosphoSiteiP50247.
SwissPalmiP50247.

2D gel databases

REPRODUCTION-2DPAGEP50247.

Proteomic databases

EPDiP50247.
PaxDbiP50247.
PeptideAtlasiP50247.
PRIDEiP50247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054607; ENSMUSP00000061851; ENSMUSG00000027597.
ENSMUST00000059524; ENSMUSP00000127198; ENSMUSG00000048087.
GeneIDi11615.
269378.
KEGGimmu:11615.
mmu:269378.
UCSCiuc008nka.2. mouse.

Organism-specific databases

CTDi191.
MGIiMGI:87968. Ahcy.

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
InParanoidiP50247.
KOiK01251.
OMAiKSDQYAV.
OrthoDBiEOG091G06EB.
PhylomeDBiP50247.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.
ReactomeiR-MMU-156581. Methylation.
R-MMU-1614635. Sulfur amino acid metabolism.

Miscellaneous databases

PROiP50247.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027597.
CleanExiMM_AHCY.
ExpressionAtlasiP50247. baseline and differential.
GenevisibleiP50247. MM.

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. 1 hit.
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_MOUSE
AccessioniPrimary (citable) accession number: P50247
Secondary accession number(s): Q91WF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.