Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10760

- SAHH_RAT

UniProt

P10760 - SAHH_RAT

Protein

Adenosylhomocysteinase

Gene

Ahcy

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 – 2431NAD1 Publication
    Binding sitei248 – 2481NAD1 Publication
    Binding sitei346 – 3461NAD1 Publication
    Binding sitei353 – 3531NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi157 – 1593NAD1 Publication
    Nucleotide bindingi222 – 2276NAD1 Publication
    Nucleotide bindingi299 – 3013NAD1 Publication
    Nucleotide bindingi426 – 4305NAD1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

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

    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

    GO - Cellular componenti

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

    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 – 11RemovedBy similarity
    Chaini2 – 432431AdenosylhomocysteinasePRO_0000116905Add
    BLAST

    Proteomic databases

    PaxDbiP10760.
    PRIDEiP10760.

    2D gel databases

    World-2DPAGE0004:P10760.

    PTM databases

    PhosphoSiteiP10760.

    Expressioni

    Gene expression databases

    GenevestigatoriP10760.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    432
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10760.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the adenosylhomocysteinase family.Curated

    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

    « Hide

    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: October 1, 2014
    This is version 145 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