Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

• HOME
• SETUP
• FAQ
• ABOUT
• GLOSSARY
• WHAT'S NEW
• FEEDBACK

AdoHcyase_NAD S-adenosyl-L-homocysteine hydrolase, NAD binding domain

SMART accession number:	SM00997
Description:	-
Interpro abstract (IPR015878):	S-adenosyl-L-homocysteine hydrolase ( EC 3.3.1.1 ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD + as a cofactor. AdoHcyase is a highly conserved protein [ (PUBMED:1631127) ] of about 430 to 470 amino acids. This entry represents the glycine-rich region in the central part of AdoHcyase, which is thought to be involved in NAD-binding [ (PUBMED:1631127) ].
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 17321 AdoHcyase_NAD domains in 17318 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing AdoHcyase_NAD domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with AdoHcyase_NAD domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing AdoHcyase_NAD domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Sganga MW, Aksamit RR, Cantoni GL, Bauer CE
  • Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteinehydrolase from Rhodobacter capsulatus.
  • Proc Natl Acad Sci U S A. 1992; 89: 6328-32
  • Display abstract

  • The genetic locus ahcY, encoding the enzyme S-adenosyl-L-homocysteinehydrolase (EC 3.3.1.1) from the bacterium Rhodobacter capsulatus, has beenmapped by mutational analysis to within a cluster of genes involved inregulating the induction and maintenance of the bacterial photosyntheticapparatus. Sequence analysis demonstrates that ahcY encodes a 51-kDapolypeptide that displays 64% sequence identity to its human homolog.Insertion mutants in ahcY lack detectable S-adenosyl-L-homocysteinehydrolase activity and, as a consequence, S-adenosyl-L-homocysteineaccumulates in the cells, resulting in a 16-fold decrease in theintracellular ratio of S-adenosyl-L-methionine toS-adenosyl-L-homocysteine as compared to wild-type cells. The ahcYdisrupted strain fails to grow in minimal medium; however, growth isrestored in minimal medium supplemented with methionine or homocysteine orin a complex medium, thereby indicating that the hydrolysis ofS-adenosyl-L-homocysteine plays a key role in the metabolism ofsulfur-containing amino acids. The ahcY mutant, when grown in supplementedmedium, synthesizes significantly reduced levels of bacteriochlorophyll,indicating that modulation of the intracellular ratio ofS-adenosyl-L-methionine to S-adenosyl-L-homocysteine may be an importantfactor in regulating bacteriochlorophyll biosynthesis.

• Structure (3D structures containing this domain)

• 3D Structures of AdoHcyase_NAD domains in PDB

  PDB code	Main view	Title
  1a7a		STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH
  1b3r		RAT LIVER S-ADENOSYLHOMOCYSTEIN HYDROLASE
  1d4f		CRYSTAL STRUCTURE OF RECOMBINANT RAT-LIVER D244E MUTANT S-ADENOSYLHOMOCYSTEINE HYDROLASE
  1k0u		Inhibition of S-adenosylhomocysteine Hydrolase by ""acyclic sugar"" Adenosine Analogue D-eritadenine
  1ky4		S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints
  1ky5		D244E mutant S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints
  1li4		Human S-adenosylhomocysteine hydrolase complexed with neplanocin
  1v8b		Crystal structure of a hydrolase
  1xwf		K185N mutated S-adenosylhomocysteine hydrolase
  2h5l		S-Adenosylhomocysteine hydrolase containing NAD and 3-deaza-D-eritadenine
  2ziz		Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3-deazaadenosine
  2zj0		Crystal structure of Mycobacterium tuberculosis S-Adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 2-fluoroadenosine
  2zj1		Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and 3'-keto-aristeromycin
  3ce6		Crystal structure of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with NAD and adenosine
  3d64		Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei
  3dhy		Crystal Structures of Mycobacterium tuberculosis S-Adenosyl-L-Homocysteine Hydrolase in Ternary Complex with Substrate and Inhibitors
  3g1u		Crystal structure of Leishmania major S-adenosylhomocysteine hydrolase
  3glq		Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furansyl-adenine
  3gvp		Human SAHH-like domain of human adenosylhomocysteinase 3
  3h9u		S-adenosyl homocysteine hydrolase (SAHH) from Trypanosoma brucei
  3mtg		Crystal structure of human S-adenosyl homocysteine hydrolase-like 1 protein
  3n58		Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
  3nj4		Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase
  3ond		Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine
  3one		Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenine
  3onf		Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin
  3x2e		3X2E
  3x2f		3X2F
  4lvc		4LVC
  4pfj		4PFJ
  4pgf		4PGF
  4yvf		4YVF
  5axa		5AXA
  5axb		5AXB
  5axc		5AXC
  5axd		5AXD
  5hm8		5HM8
  5jpi		5JPI
  5jxw		5JXW
  5t8k		5T8K
  5tj9		5TJ9
  5tls		5TLS

• Links (links to other resources describing this domain)

• INTERPRO	IPR015878
  PFAM	AdoHcyase_NAD

Send comments to Ivica Letunic