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Q9ZFE7 (MTND_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:
Acireductone dioxygenase
Alternative name(s):
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
Short name=DHK-MTPene dioxygenase
Acireductone dioxygenase (Fe(2+)-requiring)
Short name=ARD'
Short name=Fe-ARD
EC=1.13.11.54
Acireductone dioxygenase (Ni(2+)-requiring)
Short name=ARD
Short name=Ni-ARD
EC=1.13.11.53
Gene names
Name:mtnD
Synonyms:masB
OrganismKlebsiella oxytoca
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. Ref.3

Catalytic activity

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO. Ref.3

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate.

Cofactor

Binds 1 iron ion per monomer. Can be replaced by magnesium ion, but with lower activity. Ref.2 Ref.4 Ref.5 Ref.6

Binds 1 nickel ion per monomer. Can be replaced by manganese or cobalt ions. Ref.2 Ref.4 Ref.5 Ref.6

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6. HAMAP-Rule MF_01682

Subunit structure

Monomer. Ref.4 Ref.6 Ref.8

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Biophysicochemical properties

Kinetic parameters:

KM=50 µM for 1,2-dihydroxy-3-keto-1-hexene (with Ni-ARD) Ref.4

KM=52 µM for 1,2-dihydroxy-3-keto-1-hexene (with Fe-ARD)

KM=47 µM for oxygene (with Fe-ARD)

KM=110 µM for oxygene (with Ni-ARD)

Mass spectrometry

Molecular mass is 20252 Da from positions 2 - 180. Determined by ESI. Ni-ARD. Ref.2 Ref.4

Molecular mass is 20238 Da from positions 2 - 180. Determined by ESI. Fe-ARD. Ref.2

Molecular mass is 20236 Da from positions 2 - 180. Determined by ESI. Fe-ARD. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180Acireductone dioxygenase HAMAP-Rule MF_01682
PRO_0000359200

Sites

Metal binding971Iron; alternate
Metal binding971Nickel; alternate
Metal binding991Iron; alternate
Metal binding991Nickel; alternate
Metal binding1031Iron; alternate
Metal binding1031Nickel; alternate
Metal binding1411Iron; alternate
Metal binding1411Nickel; alternate
Site961May play a role in metal incorporation in vivo
Site1021May play a role in transmitting local conformational changes
Site1051Important to generate the dianion

Experimental info

Mutagenesis961E → A: Loss of dioxygenase activity and decrease in expression of soluble protein. Ref.5
Mutagenesis971H → A: Loss of dioxygenase activity and strong decrease in expression of soluble protein. Ref.5
Mutagenesis991H → A: Loss of dioxygenase activity and decrease in expression of soluble protein. Ref.5
Mutagenesis991H → S: Loss of dioxygenase activity, and little affinity for either Ni(2+) or Fe(3+) ions. Ref.5
Mutagenesis1011E → A: Strong decrease in dioxygenase activity. Exhibits high affinity for both Ni(2+) and Fe(3+) ions, but the activities of both Ni(2+)- and Fe(3+)-reconstituted mutant are considerably lower than wild-type enzymes. Ref.5
Mutagenesis1021D → A: Shows a slight decrease in dioxygenase activity and high affinity for both Ni(2+) and Fe(3+) ions. Ref.5
Mutagenesis1031E → A: Loss of dioxygenase activity and strong decrease in expression of soluble protein. Ref.5
Mutagenesis1411H → A: No expression of soluble protein. Ref.5
Mutagenesis1411H → F: Strong decrease in expression of soluble protein. Ref.5

Secondary structure

................................. 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZFE7 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 7EC4B7E668C91F14

FASTA18020,329
        10         20         30         40         50         60 
MSALTIFSVK DPQNSLWHST NAEEIQQQLN AKGVRFERWQ ADRDLGAAPT AETVIAAYQH 

        70         80         90        100        110        120 
AIDKLVAEKG YQSWDVISLR ADNPQKEALR EKFLNEHTHG EDEVRFFVEG AGLFCLHIGD 

       130        140        150        160        170        180 
EVFQVLCEKN DLISVPAHTP HWFDMGSEPN FTAIRIFDNP EGWIAQFTGD DIASAYPRLA 

« Hide

References

[1]"Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca."
Balakrishnan R., Frohlich M., Rahaim P.T., Backman K., Yocum R.R.
J. Biol. Chem. 268:24792-24795(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
Strain: M5a1.
[2]"One protein, two enzymes."
Dai Y., Wensink P.C., Abeles R.H.
J. Biol. Chem. 274:1193-1195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-180, PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY, COFACTOR.
Strain: UNF932.
[3]"A bacterial enzyme that catalyzes formation of carbon monoxide."
Wray J.W., Abeles R.H.
J. Biol. Chem. 268:21466-21469(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[4]"Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae."
Dai Y., Pochapsky T.C., Abeles R.H.
Biochemistry 40:6379-6387(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724."
Chai S.C., Ju T., Dang M., Goldsmith R.B., Maroney M.J., Pochapsky T.C.
Biochemistry 47:2428-2438(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-96; HIS-97; HIS-99; GLU-101; ASP-102; GLU-103 AND HIS-141, COFACTOR.
[6]"Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae."
Pochapsky T.C., Pochapsky S.S., Ju T., Mo H., Al-Mjeni F., Maroney M.J.
Nat. Struct. Biol. 9:966-972(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, SUBUNIT, COFACTOR.
[7]"A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings."
Pochapsky T.C., Pochapsky S.S., Ju T., Hoefler C., Liang J.
J. Biomol. NMR 34:117-127(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[8]"One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase."
Ju T., Goldsmith R.B., Chai S.C., Maroney M.J., Pochapsky S.S., Pochapsky T.C.
J. Mol. Biol. 363:823-834(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00148 Genomic DNA. Translation: AAC43184.1.
AF102514 Genomic DNA. Translation: AAD11793.1.
PIRA59159.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZRRNMR-A2-180[»]
2HJINMR-A2-180[»]
ProteinModelPortalQ9ZFE7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-1323.
BRENDA1.13.11.54. 2811.
UniPathwayUPA00904; UER00878.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
HAMAPMF_01682. Salvage_MtnD.
InterProIPR023956. Acireductn_d0ase.
IPR004313. Acireductn_dOase_family.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR23418. PTHR23418. 1 hit.
PfamPF03079. ARD. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZFE7.

Entry information

Entry nameMTND_KLEOX
AccessionPrimary (citable) accession number: Q9ZFE7
Secondary accession number(s): Q48390
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: February 19, 2014
This is version 65 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways