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P05102 (MTH1_HAEPH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase HhaI

Short name=M.HhaI
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase HhaI
Gene names
Name:hhaIM
OrganismHaemophilus parahaemolyticus
Taxonomic identifier735 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Subunit structure

Monomer.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Caution

Strain ATCC 10014 was originally thought to originate from H.haemolyticus.

Biophysicochemical properties

Kinetic parameters:

KM=69 nM for DNA Ref.3

KM=15 nM for S-adenosyl-L-methionine (SAM)

Vmax=87.0 nmol/min/mg enzyme

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Modification methylase HhaI
PRO_0000087882

Regions

Domain12 – 325314SAM-dependent MTase C5-type

Sites

Active site811

Experimental info

Mutagenesis2371Q → X: Decrease in enzyme activity due to 98%-99% loss of DNA-binding activity. No change in substrate specificity. Ref.3

Secondary structure

................................................................. 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05102 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: EF8A297E1DF819EB

FASTA32736,996
        10         20         30         40         50         60 
MIEIKDKQLT GLRFIDLFAG LGGFRLALES CGAECVYSNE WDKYAQEVYE MNFGEKPEGD 

        70         80         90        100        110        120 
ITQVNEKTIP DHDILCAGFP CQAFSISGKQ KGFEDSRGTL FFDIARIVRE KKPKVVFMEN 

       130        140        150        160        170        180 
VKNFASHDNG NTLEVVKNTM NELDYSFHAK VLNALDYGIP QKRERIYMIC FRNDLNIQNF 

       190        200        210        220        230        240 
QFPKPFELNT FVKDLLLPDS EVEHLVIDRK DLVMTNQEIE QTTPKTVRLG IVGKGGQGER 

       250        260        270        280        290        300 
IYSTRGIAIT LSAYGGGIFA KTGGYLVNGK TRKLHPRECA RVMGYPDSYK VHPSTSQAYK 

       310        320 
QFGNSVVINV LQYIAYNIGS SLNFKPY 

« Hide

References

[1]"Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase."
Caserta M., Zacharias W., Nwankwo D.O., Wilson G.G., Wells R.D.
J. Biol. Chem. 262:4770-4777(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10014 / CCUG 3716 / NCTC 8479.
[2]"The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center."
Mi S., Roberts R.J.
Nucleic Acids Res. 21:2459-2464(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[3]"Functional analysis of Gln-237 mutants of HhaI methyltransferase."
Mi S., Alonso D., Roberts R.J.
Nucleic Acids Res. 23:620-627(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-237.
[4]"Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine."
Cheng X., Kumar S., Posfai J., Pflugrath J.W., Roberts R.J.
Cell 74:299-307(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"HhaI methyltransferase flips its target base out of the DNA helix."
Klimasauskas S., Kumar S., Roberts R.J., Cheng X.
Cell 76:357-369(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase."
Kumar S., Horton J.R., Jones G.D., Walker R.T., Roberts R.J., Cheng X.
Nucleic Acids Res. 25:2773-2783(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[7]"Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base."
O'Gara M., Horton J.R., Roberts R.J., Cheng X.
Nat. Struct. Biol. 5:872-877(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
[8]"Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide."
O'Gara M., Zhang X., Roberts R.J., Cheng X.
J. Mol. Biol. 287:201-209(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02677 Genomic DNA. Translation: AAA24989.1.
PIRXYHIH1. A26260.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
10MHX-ray2.55A1-327[»]
1FJXX-ray2.26A1-327[»]
1HMYX-ray2.50A1-327[»]
1M0EX-ray2.50A1-327[»]
1MHTX-ray2.60A1-327[»]
1SKMX-ray2.20A1-327[»]
1SVUX-ray2.66A/B1-327[»]
2C7OX-ray1.90A1-327[»]
2C7PX-ray1.70A1-327[»]
2C7QX-ray1.85A1-327[»]
2C7RX-ray1.90A1-327[»]
2HMYX-ray2.61B1-327[»]
2HR1X-ray1.96A1-327[»]
2I9KX-ray2.65A1-327[»]
2UYCX-ray2.00A1-327[»]
2UYHX-ray2.63A1-327[»]
2UZ4X-ray2.10A1-327[»]
2Z6AX-ray2.88A1-327[»]
2Z6QX-ray2.79A1-327[»]
2Z6UX-ray2.72A1-327[»]
2ZCJX-ray2.75A1-327[»]
3EEOX-ray1.94A1-327[»]
3MHTX-ray2.70A1-327[»]
4MHTX-ray2.70A1-327[»]
5MHTX-ray2.70A1-327[»]
6MHTX-ray2.05A1-327[»]
7MHTX-ray2.87A1-327[»]
8MHTX-ray2.76A1-327[»]
9MHTX-ray2.39A1-327[»]
ProteinModelPortalP05102.
SMRP05102. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3421. M.HhaI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05102.

Entry information

Entry nameMTH1_HAEPH
AccessionPrimary (citable) accession number: P05102
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references