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Protein

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2

Gene

PHYPADRAFT_134384

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).UniRule annotation

Catalytic activityi

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

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per monomer. Can also use other divalent metal cations.UniRule annotation

Pathway: L-methionine biosynthesis via salvage pathway

This protein is involved in step 5 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 (PHYPADRAFT_111231)
  3. Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 (PHYPADRAFT_111231)
  4. Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 (PHYPADRAFT_111231)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 3 (PHYPADRAFT_164159), Uncharacterized protein (PHYPADRAFT_111075), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (PHYPADRAFT_146733), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 1 (PHYPADRAFT_128349), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2 (PHYPADRAFT_134384), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (PHYPADRAFT_71444)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron or nickelUniRule annotation
Metal bindingi96 – 961Iron or nickelUniRule annotation
Metal bindingi100 – 1001Iron or nickelUniRule annotation
Metal bindingi139 – 1391Iron or nickelUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00904; UER00878.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2UniRule annotation (EC:1.13.11.54UniRule annotation)
Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring) 2UniRule annotation
Short name:
ARD 2UniRule annotation
Short name:
Fe-ARD 2UniRule annotation
Gene namesi
ORF Names:PHYPADRAFT_134384
OrganismiPhyscomitrella patens subsp. patens (Moss)
Taxonomic identifieri3218 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
ProteomesiUP000006727 Componenti: Partially assembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1951951,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2PRO_0000414343Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi3218.PP1S111_19V6.1.

Structurei

3D structure databases

ProteinModelPortaliA9SS00.
SMRiA9SS00. Positions 8-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acireductone dioxygenase (ARD) family.UniRule annotation

Phylogenomic databases

InParanoidiA9SS00.
KOiK08967.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_03154. Salvage_MtnD_euk.
InterProiIPR004313. Acireductn_dOase_family.
IPR027496. MTCBP-1_eukaryotes.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR23418. PTHR23418. 1 hit.
PfamiPF03079. ARD. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

A9SS00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVQRPPLEA WYMNDSEEDQ RLPHHRNPPE YVTLEKLAAL GVIHWVLDAD
60 70 80 90 100
NHETDPELSI IRKDRGYNYT DVITVCPEML PSYEAKIKSF YEEHIHMDEE
110 120 130 140 150
IRYCLDGSGY FDVRDPEDHW IRIWVRKGDM IVLPAGCYHR FTLDEHNYIM
160 170 180 190
AMRLFVGEPI WTPYNRPQDE HPVRKGYVHQ FLQPELLDVD MSISA
Length:195
Mass (Da):23,199
Last modified:February 5, 2008 - v1
Checksum:iD0AED4C8E9A82C70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS545000 Genomic DNA. Translation: EDQ66042.1.
RefSeqiXP_001769170.1. XM_001769118.1.

Genome annotation databases

GeneIDi5932378.
KEGGippp:PHYPADRAFT_134384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS545000 Genomic DNA. Translation: EDQ66042.1.
RefSeqiXP_001769170.1. XM_001769118.1.

3D structure databases

ProteinModelPortaliA9SS00.
SMRiA9SS00. Positions 8-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3218.PP1S111_19V6.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5932378.
KEGGippp:PHYPADRAFT_134384.

Phylogenomic databases

InParanoidiA9SS00.
KOiK08967.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00878.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_03154. Salvage_MtnD_euk.
InterProiIPR004313. Acireductn_dOase_family.
IPR027496. MTCBP-1_eukaryotes.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR23418. PTHR23418. 1 hit.
PfamiPF03079. ARD. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
    Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
    , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
    Science 319:64-69(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Gransden 2004.

Entry informationi

Entry nameiMTND2_PHYPA
AccessioniPrimary (citable) accession number: A9SS00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: February 5, 2008
Last modified: June 24, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.