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Protein

Adenosylhomocysteinase

Gene

Ahcy

Organism
Rattus norvegicus (Rat)
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+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication

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 2 (Ahcyl1), Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase (Ahcy)
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 sitei57Substrate1
Binding sitei131Substrate1
Binding sitei156Substrate1
Binding sitei186Substrate1
Binding sitei190Substrate1
Binding sitei243NAD1 Publication1
Binding sitei248NAD1 Publication1
Binding sitei346NAD1 Publication1
Binding sitei353NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi157 – 159NAD1 Publication3
Nucleotide bindingi222 – 227NAD1 Publication6
Nucleotide bindingi299 – 301NAD1 Publication3
Nucleotide bindingi426 – 430NAD1 Publication5

GO - Molecular functioni

  • adenosylhomocysteinase activity Source: RGD
  • adenosylselenohomocysteinase activity Source: Reactome
  • adenyl nucleotide binding Source: RGD
  • identical protein binding Source: RGD
  • NAD binding Source: RGD

GO - Biological processi

  • chronic inflammatory response to antigenic stimulus Source: RGD
  • circadian sleep/wake cycle Source: RGD
  • homocysteine biosynthetic process Source: RGD
  • one-carbon metabolic process Source: UniProtKB-KW
  • response to hypoxia Source: RGD
  • response to nutrient Source: RGD
  • S-adenosylhomocysteine catabolic process Source: RGD
  • S-adenosylmethionine cycle Source: GO_Central
  • selenium compound metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8582.
BRENDAi3.3.1.1. 5301.
3.5.4.28. 5301.
ReactomeiR-RNO-156581. Methylation.
R-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
SABIO-RKP10760.
UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylhomocysteinase (EC:3.3.1.1)
Short name:
AdoHcyase
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Gene namesi
Name:Ahcy
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi69260. Ahcy.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • neuron projection Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi131D → N: Strongly reduces activity. 1 Publication1
Mutagenesisi186K → N: Strongly reduces activity. 1 Publication1
Mutagenesisi190D → N: Strongly reduces activity. 1 Publication1
Mutagenesisi191N → S: Strongly reduces activity. 1 Publication1
Mutagenesisi245D → E: Changes active site geometry and alters affinity for NAD. 1

Chemistry databases

ChEMBLiCHEMBL3118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001169052 – 432AdenosylhomocysteinaseAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei183PhosphoserineBy similarity1
Modified residuei193PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP10760.
PRIDEiP10760.

2D gel databases

World-2DPAGE0004:P10760.

PTM databases

iPTMnetiP10760.
PhosphoSitePlusiP10760.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017777.
GenevisibleiP10760. RN.

Interactioni

Subunit structurei

Homotetramer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

BioGridi248089. 1 interactor.
IntActiP10760. 1 interactor.
MINTiMINT-4570399.
STRINGi10116.ENSRNOP00000024310.

Chemistry databases

BindingDBiP10760.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Turni12 – 14Combined sources3
Helixi15 – 25Combined sources11
Helixi26 – 28Combined sources3
Helixi30 – 39Combined sources10
Turni40 – 42Combined sources3
Turni44 – 47Combined sources4
Beta strandi49 – 54Combined sources6
Helixi58 – 69Combined sources12
Beta strandi73 – 77Combined sources5
Turni81 – 83Combined sources3
Helixi86 – 94Combined sources9
Beta strandi99 – 101Combined sources3
Helixi107 – 116Combined sources10
Beta strandi118 – 120Combined sources3
Beta strandi127 – 133Combined sources7
Helixi134 – 142Combined sources9
Helixi144 – 147Combined sources4
Beta strandi152 – 155Combined sources4
Helixi158 – 169Combined sources12
Beta strandi177 – 179Combined sources3
Helixi180 – 182Combined sources3
Helixi184 – 190Combined sources7
Helixi192 – 207Combined sources16
Beta strandi215 – 219Combined sources5
Helixi223 – 234Combined sources12
Beta strandi238 – 242Combined sources5
Helixi246 – 253Combined sources8
Turni254 – 256Combined sources3
Beta strandi258 – 260Combined sources3
Helixi262 – 265Combined sources4
Turni266 – 268Combined sources3
Beta strandi270 – 274Combined sources5
Beta strandi277 – 279Combined sources3
Helixi284 – 287Combined sources4
Beta strandi294 – 298Combined sources5
Turni302 – 304Combined sources3
Helixi308 – 314Combined sources7
Beta strandi315 – 322Combined sources8
Beta strandi325 – 330Combined sources6
Beta strandi335 – 339Combined sources5
Helixi340 – 342Combined sources3
Helixi345 – 349Combined sources5
Helixi355 – 374Combined sources20
Turni376 – 378Combined sources3
Beta strandi381 – 385Combined sources5
Helixi388 – 398Combined sources11
Turni399 – 402Combined sources4
Helixi411 – 417Combined sources7
Beta strandi421 – 423Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B3RX-ray2.80A/B/C/D2-432[»]
1D4FX-ray2.80A/B/C/D2-432[»]
1K0UX-ray3.00A/B/C/D/E/F/G/H2-432[»]
1KY4X-ray2.80A/B/C/D2-432[»]
1KY5X-ray2.80A/B/C/D2-432[»]
1XWFX-ray2.80A/B/C/D2-432[»]
2H5LX-ray2.80A/B/C/D/E/F/G/H2-432[»]
ProteinModelPortaliP10760.
SMRiP10760.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10760.

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
InParanoidiP10760.
KOiK01251.
OMAiVHDKYPQ.
OrthoDBiEOG091G06EB.
PhylomeDBiP10760.
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. 2 hits.
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.

P10760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI
60 70 80 90 100
AGCLHMTVET AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF
110 120 130 140 150
AWKGETDEEY LWCIEQTLHF KDGPLNMILD DGGDLTNLIH TKHPQLLSGI
160 170 180 190 200
RGISEETTTG VHNLYKMMAN 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 IKPQVDRYLL KNGHRIILLA EGRLVNLGCA
360 370 380 390 400
MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG
410 420 430
KLNVKLTKLT EKQAQYLGMP INGPFKPDHY RY
Length:432
Mass (Da):47,538
Last modified:January 23, 2007 - v3
Checksum:i93CA5BED07B4FCDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15185 mRNA. Translation: AAA40705.1.
U14937 Genomic DNA. Translation: AAA92043.1.
PIRiA26583.
RefSeqiNP_058897.1. NM_017201.1.
UniGeneiRn.5878.

Genome annotation databases

EnsembliENSRNOT00000024310; ENSRNOP00000024310; ENSRNOG00000017777.
GeneIDi29443.
KEGGirno:29443.
UCSCiRGD:69260. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15185 mRNA. Translation: AAA40705.1.
U14937 Genomic DNA. Translation: AAA92043.1.
PIRiA26583.
RefSeqiNP_058897.1. NM_017201.1.
UniGeneiRn.5878.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B3RX-ray2.80A/B/C/D2-432[»]
1D4FX-ray2.80A/B/C/D2-432[»]
1K0UX-ray3.00A/B/C/D/E/F/G/H2-432[»]
1KY4X-ray2.80A/B/C/D2-432[»]
1KY5X-ray2.80A/B/C/D2-432[»]
1XWFX-ray2.80A/B/C/D2-432[»]
2H5LX-ray2.80A/B/C/D/E/F/G/H2-432[»]
ProteinModelPortaliP10760.
SMRiP10760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248089. 1 interactor.
IntActiP10760. 1 interactor.
MINTiMINT-4570399.
STRINGi10116.ENSRNOP00000024310.

Chemistry databases

BindingDBiP10760.
ChEMBLiCHEMBL3118.

PTM databases

iPTMnetiP10760.
PhosphoSitePlusiP10760.

2D gel databases

World-2DPAGE0004:P10760.

Proteomic databases

PaxDbiP10760.
PRIDEiP10760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024310; ENSRNOP00000024310; ENSRNOG00000017777.
GeneIDi29443.
KEGGirno:29443.
UCSCiRGD:69260. rat.

Organism-specific databases

CTDi191.
RGDi69260. Ahcy.

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
InParanoidiP10760.
KOiK01251.
OMAiVHDKYPQ.
OrthoDBiEOG091G06EB.
PhylomeDBiP10760.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.
BioCyciMetaCyc:MONOMER-8582.
BRENDAi3.3.1.1. 5301.
3.5.4.28. 5301.
ReactomeiR-RNO-156581. Methylation.
R-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
SABIO-RKP10760.

Miscellaneous databases

EvolutionaryTraceiP10760.
PROiP10760.

Gene expression databases

BgeeiENSRNOG00000017777.
GenevisibleiP10760. RN.

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. 2 hits.
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_RAT
AccessioniPrimary (citable) accession number: P10760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 165 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

3D-structure, Complete proteome, Direct protein sequencing, 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.