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P10760

- SAHH_RAT

UniProt

P10760 - SAHH_RAT

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Protein
Adenosylhomocysteinase
Gene
Ahcy
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 NAD per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571Substrate
Binding sitei131 – 1311Substrate
Binding sitei156 – 1561Substrate
Binding sitei186 – 1861Substrate
Binding sitei190 – 1901Substrate
Binding sitei243 – 2431NAD
Binding sitei248 – 2481NAD
Binding sitei346 – 3461NAD
Binding sitei353 – 3531NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi157 – 1593NADUniRule annotation
Nucleotide bindingi222 – 2276NADUniRule annotation
Nucleotide bindingi299 – 3013NADUniRule annotation
Nucleotide bindingi426 – 4305NADUniRule annotation

GO - Molecular functioni

  1. NAD binding Source: RGD
  2. adenosylhomocysteinase activity Source: RGD
  3. adenyl nucleotide binding Source: RGD
  4. identical protein binding Source: RGD

GO - Biological processi

  1. S-adenosylhomocysteine catabolic process Source: RGD
  2. chronic inflammatory response to antigenic stimulus Source: RGD
  3. circadian sleep/wake cycle Source: RGD
  4. homocysteine biosynthetic process Source: RGD
  5. one-carbon metabolic process Source: UniProtKB-KW
  6. response to hypoxia Source: RGD
  7. response to nutrient Source: RGD
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.
ReactomeiREACT_194782. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi69260. Ahcy.

Subcellular locationi

Cytoplasm. Melanosome By similarity UniRule annotation

GO - Cellular componenti

  1. cytosol Source: RGD
  2. melanosome Source: UniProtKB-SubCell
  3. neuron projection Source: RGD
  4. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311D → N: Strongly reduces activity. 1 Publication
Mutagenesisi186 – 1861K → N: Strongly reduces activity. 1 Publication
Mutagenesisi190 – 1901D → N: Strongly reduces activity. 1 Publication
Mutagenesisi191 – 1911N → S: Strongly reduces activity. 1 Publication
Mutagenesisi245 – 2451D → E: Changes active site geometry and alters affinity for NAD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 432431AdenosylhomocysteinaseUniRule annotation
PRO_0000116905Add
BLAST

Proteomic databases

PaxDbiP10760.
PRIDEiP10760.

2D gel databases

World-2DPAGE0004:P10760.

PTM databases

PhosphoSiteiP10760.

Expressioni

Gene expression databases

GenevestigatoriP10760.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103
Turni12 – 143
Helixi15 – 2511
Helixi26 – 283
Helixi30 – 3910
Turni40 – 423
Turni44 – 474
Beta strandi49 – 546
Helixi58 – 6912
Beta strandi73 – 775
Turni81 – 833
Helixi86 – 949
Beta strandi99 – 1013
Helixi107 – 11610
Beta strandi118 – 1203
Beta strandi127 – 1337
Helixi134 – 1429
Helixi144 – 1474
Beta strandi152 – 1554
Helixi158 – 16912
Beta strandi177 – 1793
Helixi180 – 1823
Helixi184 – 1907
Helixi192 – 20716
Beta strandi215 – 2195
Helixi223 – 23412
Beta strandi238 – 2425
Helixi246 – 2538
Turni254 – 2563
Beta strandi258 – 2603
Helixi262 – 2654
Turni266 – 2683
Beta strandi270 – 2745
Beta strandi277 – 2793
Helixi284 – 2874
Beta strandi294 – 2985
Turni302 – 3043
Helixi308 – 3147
Beta strandi315 – 3228
Beta strandi325 – 3306
Beta strandi335 – 3395
Helixi340 – 3423
Helixi345 – 3495
Helixi355 – 37420
Turni376 – 3783
Beta strandi381 – 3855
Helixi388 – 39811
Turni399 – 4024
Helixi411 – 4177
Beta strandi421 – 4233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 3-432.

Miscellaneous databases

EvolutionaryTraceiP10760.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
InParanoidiP10760.
KOiK01251.
OMAiMETRRKY.
OrthoDBiEOG76739S.
PhylomeDBiP10760.
TreeFamiTF300415.

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. 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]
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

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MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI    50
AGCLHMTVET AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF 100
AWKGETDEEY LWCIEQTLHF KDGPLNMILD DGGDLTNLIH TKHPQLLSGI 150
RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI 200
DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL 250
QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG 300
HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA 350
MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG 400
KLNVKLTKLT EKQAQYLGMP INGPFKPDHY RY 432
Length:432
Mass (Da):47,538
Last modified:January 23, 2007 - v3
Checksum:i93CA5BED07B4FCDE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M15185 mRNA. Translation: AAA40705.1 .
U14937 Genomic DNA. Translation: AAA92043.1 .
PIRi A26583.
RefSeqi NP_058897.1. NM_017201.1.
UniGenei Rn.5878.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B3R X-ray 2.80 A/B/C/D 2-432 [» ]
1D4F X-ray 2.80 A/B/C/D 2-432 [» ]
1K0U X-ray 3.00 A/B/C/D/E/F/G/H 2-432 [» ]
1KY4 X-ray 2.80 A/B/C/D 2-432 [» ]
1KY5 X-ray 2.80 A/B/C/D 2-432 [» ]
1XWF X-ray 2.80 A/B/C/D 2-432 [» ]
2H5L X-ray 2.80 A/B/C/D/E/F/G/H 2-432 [» ]
ProteinModelPortali P10760.
SMRi P10760. Positions 3-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248089. 1 interaction.
IntActi P10760. 1 interaction.
MINTi MINT-4570399.
STRINGi 10116.ENSRNOP00000024310.

Chemistry

BindingDBi P10760.
ChEMBLi CHEMBL3118.

PTM databases

PhosphoSitei P10760.

2D gel databases

World-2DPAGE 0004:P10760.

Proteomic databases

PaxDbi P10760.
PRIDEi P10760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000024310 ; ENSRNOP00000024310 ; ENSRNOG00000017777 .
GeneIDi 29443.
KEGGi rno:29443.
UCSCi RGD:69260. rat.

Organism-specific databases

CTDi 191.
RGDi 69260. Ahcy.

Phylogenomic databases

eggNOGi COG0499.
GeneTreei ENSGT00390000003626.
HOGENOMi HOG000227987.
HOVERGENi HBG005041.
InParanoidi P10760.
KOi K01251.
OMAi METRRKY.
OrthoDBi EOG76739S.
PhylomeDBi P10760.
TreeFami TF300415.

Enzyme and pathway databases

UniPathwayi UPA00314 ; UER00076 .
BioCyci MetaCyc:MONOMER-8582.
BRENDAi 3.3.1.1. 5301.
Reactomei REACT_194782. Sulfur amino acid metabolism.
SABIO-RK P10760.

Miscellaneous databases

EvolutionaryTracei P10760.
NextBioi 609197.
PROi P10760.

Gene expression databases

Genevestigatori P10760.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00563. AdoHcyase.
InterProi IPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view ]
PANTHERi PTHR23420. PTHR23420. 1 hit.
Pfami PF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTi SM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00936. ahcY. 1 hit.
PROSITEi PS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence."
    Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund P.S. Jr., Aksamit R.R., Unson C.G., Cantoni G.L.
    Proc. Natl. Acad. Sci. U.S.A. 84:719-723(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase."
    Merta A., Aksamit R.R., Kasir J., Cantoni G.L.
    Eur. J. Biochem. 229:575-582(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Fischer 344.
  3. "S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5'-p-fluorosulfonylbenzoyladenosine."
    Gomi T., Ogawa H., Fujioka M.
    J. Biol. Chem. 261:13422-13425(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-94.
  4. Lubec G., Afjehi-Sadat L., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 143-151 AND 268-285, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  5. "Crystal structure of S-adenosylhomocysteine hydrolase from rat liver."
    Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.
    Biochemistry 38:8323-8333(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, SUBUNIT.
    Tissue: Liver.
  6. "Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure of D244E mutant enzyme."
    Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F.
    J. Biol. Chem. 275:32147-32156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245.
  7. "Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine hydrolase complexed with D-eritadenine."
    Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., Fujioka M., Takusagawa F.
    J. Biol. Chem. 277:7477-7482(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  8. "Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190."
    Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M., Takusagawa F.
    J. Biol. Chem. 277:22670-22676(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF ASP-131; LYS-186; ASP-190 AND ASN-191.

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: September 3, 2014
This is version 144 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

External Data

Dasty 3

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