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A7HU87 (MTND_PARL1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Plav_1853
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhodobiaceaeParvibaculum

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01682

Catalytic activity

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO. HAMAP-Rule MF_01682

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

Cofactor

Binds 1 iron ion per monomer By similarity. HAMAP-Rule MF_01682

Binds 1 nickel ion per monomer By similarity. HAMAP-Rule MF_01682

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 By similarity. HAMAP-Rule MF_01682

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Acireductone dioxygenase HAMAP-Rule MF_01682
PRO_0000359214

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A7HU87 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: DDCA09AEF14BD9AD

FASTA18420,487
        10         20         30         40         50         60 
MTHLTVYPDT DPATVLLDTR DGAEIAASLS GIGVVFERWD APHALGEDAD QTAVLAAYEA 

        70         80         90        100        110        120 
DVKRLMDEGG YKSVDVVRVK PDNPNRAEMR QKFLAEHTHD DDEVRFFVEG AGAFYLRKDG 

       130        140        150        160        170        180 
RVYRVVCERN DLISVPAGTT HWFDTGAAPH FCAIRIFTSP EGWVGHFTGD DIATRFPKFE 


SEPQ 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DS-1 / DSM 13023 / NCIMB 13966.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000774 Genomic DNA. Translation: ABS63470.1.
RefSeqYP_001413127.1. NC_009719.1.

3D structure databases

ProteinModelPortalA7HU87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402881.Plav_1853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS63470; ABS63470; Plav_1853.
GeneID5456069.
KEGGpla:Plav_1853.
PATRIC22865357. VBIParLav90819_1905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1791.
HOGENOMHOG000201072.
KOK08967.
OMAVLCEKND.
OrthoDBEOG6ZPT06.

Enzyme and pathway databases

BioCycPLAV402881:GHQA-1879-MONOMER.
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...

Entry information

Entry nameMTND_PARL1
AccessionPrimary (citable) accession number: A7HU87
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 45 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

PATHWAY comments

Index of metabolic and biosynthesis pathways