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Protein

Adenosylhomocysteinase

Gene

Ahcy

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 (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

Keywordsi

Molecular functionHydrolase
Biological processOne-carbon metabolism
LigandNAD

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
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi69260 Ahcy

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ChainiPRO_00001169051 – 432AdenosylhomocysteinaseAdd BLAST432

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
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
OMAiTGNRDII
OrthoDBiEOG091G06EB
PhylomeDBiP10760
TreeFamiTF300415

Family and domain databases

CDDicd00401 SAHH, 1 hit
HAMAPiMF_00563 AdoHcyase, 1 hit
InterProiView protein in InterPro
IPR034373 Adenosylhomocysteinase
IPR000043 Adenosylhomocysteinase-like
IPR015878 Ado_hCys_hydrolase_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020082 S-Ado-L-homoCys_hydrolase_CS
PANTHERiPTHR23420 PTHR23420, 1 hit
PfamiView protein in Pfam
PF05221 AdoHcyase, 2 hits
PF00670 AdoHcyase_NAD, 1 hit
PIRSFiPIRSF001109 Ad_hcy_hydrolase, 1 hit
SMARTiView protein in SMART
SM00996 AdoHcyase, 1 hit
SM00997 AdoHcyase_NAD, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00936 ahcY, 1 hit
PROSITEiView protein in PROSITE
PS00738 ADOHCYASE_1, 1 hit
PS00739 ADOHCYASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Similar proteinsi

Entry informationi

Entry nameiSAHH_RAT
AccessioniPrimary (citable) accession number: P10760
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 176 of the entry and version 3 of the sequence. See 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

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