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Q7V8X5 (MTND_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:PMT_0197
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length185 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 – 185185Acireductone dioxygenase HAMAP-Rule MF_01682
PRO_0000359216

Sites

Metal binding1021Iron; alternate By similarity
Metal binding1021Nickel; alternate By similarity
Metal binding1041Iron; alternate By similarity
Metal binding1041Nickel; alternate By similarity
Metal binding1081Iron; alternate By similarity
Metal binding1081Nickel; alternate By similarity
Metal binding1461Iron; alternate By similarity
Metal binding1461Nickel; alternate By similarity
Site1011May play a role in metal incorporation in vivo By similarity
Site1071May play a role in transmitting local conformational changes By similarity
Site1101Important to generate the dianion By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8X5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7F642F7459F8E8C7

FASTA18520,649
        10         20         30         40         50         60 
MSRLSIHPEG STNATSPAEP LLESDDPAVI KVELAKRGIA FQRWPAKVKL DQNSSESDIL 

        70         80         90        100        110        120 
AAYAVEIARV QADGRYPTVD AIRITPDHPD REALRQKFLD EHTHAEDEVR FFVEGCGLFC 

       130        140        150        160        170        180 
LHIGAEVLQV LCEQNDCINV PAGTRHWFDM GSKPQFCAVR FFDNPEGWIA NFTGDAIAER 


FAKLP 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20372.1.
RefSeqNP_894030.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V8X5.
SMRQ7V8X5. Positions 2-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT0197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20372; CAE20372; PMT_0197.
GeneID1729659.
KEGGpmt:PMT0197.
PATRIC23008113. VBIProMar135351_0217.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1791.
KOK08967.
OMAVLCEKND.
OrthoDBEOG6ZPT06.

Enzyme and pathway databases

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_PROMM
AccessionPrimary (citable) accession number: Q7V8X5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 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