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Protein

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

Gene

Adi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14.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 annotation1 PublicationNote: Binds 1 Fe cation per monomer. Can also use other divalent metal cations.UniRule annotation1 Publication

Pathwayi: 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. Methylthioribose-1-phosphate isomerase (Mri1)
  2. Methylthioribulose-1-phosphate dehydratase (Apip)
  3. Enolase-phosphatase E1 (Enoph1)
  4. Enolase-phosphatase E1 (Enoph1)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1)
  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 bindingi88 – 881Iron or nickel
Metal bindingi90 – 901Iron or nickel
Metal bindingi94 – 941Iron or nickel
Metal bindingi133 – 1331Iron or nickel

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

BRENDAi1.13.11.53. 3474.
1.13.11.54. 3474.
ReactomeiR-MMU-1237112. Methionine salvage pathway.
UniPathwayiUPA00904; UER00878.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseUniRule annotation (EC:1.13.11.54UniRule annotation)
Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring)UniRule annotation
Short name:
ARDUniRule annotation
Short name:
Fe-ARDUniRule annotation
Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1UniRule annotation
Short name:
MTCBP-1UniRule annotation
Gene namesi
Name:Adi1
Synonyms:Mtcbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2144929. Adi1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

  • Note: Localizes to the plasma membrane when complexed to MMP14.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1791791,2-dihydroxy-3-keto-5-methylthiopentene dioxygenasePRO_0000162943Add
BLAST

Proteomic databases

EPDiQ99JT9.
MaxQBiQ99JT9.
PaxDbiQ99JT9.
PeptideAtlasiQ99JT9.
PRIDEiQ99JT9.

PTM databases

iPTMnetiQ99JT9.
PhosphoSiteiQ99JT9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020629.
CleanExiMM_ADI1.
ExpressionAtlasiQ99JT9. baseline and differential.
GenevisibleiQ99JT9. MM.

Interactioni

Subunit structurei

Monomer. Interacts with MMP14.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020957.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi28 – 336Combined sources
Beta strandi37 – 404Combined sources
Helixi43 – 453Combined sources
Helixi50 – 5910Combined sources
Beta strandi63 – 697Combined sources
Turni71 – 733Combined sources
Helixi77 – 859Combined sources
Beta strandi94 – 10815Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi143 – 15210Combined sources
Beta strandi158 – 1603Combined sources
Helixi166 – 17611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VR3X-ray2.06A1-179[»]
5I8SX-ray1.89A1-179[»]
5I8TX-ray1.75A1-179[»]
5I8YX-ray1.94A1-179[»]
5I91X-ray1.76A1-179[»]
5I93X-ray2.24A1-179[»]
ProteinModelPortaliQ99JT9.
SMRiQ99JT9. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99JT9.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2107. Eukaryota.
COG1791. LUCA.
GeneTreeiENSGT00390000008195.
HOGENOMiHOG000201071.
HOVERGENiHBG081992.
InParanoidiQ99JT9.
KOiK08967.
OMAiWIRIAVS.
OrthoDBiEOG091G0OM4.
PhylomeDBiQ99JT9.
TreeFamiTF300231.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_03154. Salvage_MtnD_euk. 1 hit.
InterProiIPR004313. ARD.
IPR027496. ARD_euk.
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.

Q99JT9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQAWYMDES TADPRKPHRA QPDRPVSLEQ LRTLGVLYWK LDADKYENDP
60 70 80 90 100
ELEKIRKMRN YSWMDIITIC KDTLPNYEEK IKMFFEEHLH LDEEIRYILE
110 120 130 140 150
GSGYFDVRDK EDKWIRISME KGDMITLPAG IYHRFTLDEK NYVKAMRLFV
160 170
GEPVWTPYNR PADHFDARVQ YMSFLEGTA
Length:179
Mass (Da):21,524
Last modified:June 1, 2001 - v1
Checksum:i02CE7B89181EBEFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK145831 mRNA. Translation: BAE26682.1.
BC005695 mRNA. Translation: AAH05695.1.
CCDSiCCDS25853.1.
RefSeqiNP_598813.1. NM_134052.2.
UniGeneiMm.291504.

Genome annotation databases

EnsembliENSMUST00000020957; ENSMUSP00000020957; ENSMUSG00000020629.
GeneIDi104923.
KEGGimmu:104923.
UCSCiuc007nfv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK145831 mRNA. Translation: BAE26682.1.
BC005695 mRNA. Translation: AAH05695.1.
CCDSiCCDS25853.1.
RefSeqiNP_598813.1. NM_134052.2.
UniGeneiMm.291504.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VR3X-ray2.06A1-179[»]
5I8SX-ray1.89A1-179[»]
5I8TX-ray1.75A1-179[»]
5I8YX-ray1.94A1-179[»]
5I91X-ray1.76A1-179[»]
5I93X-ray2.24A1-179[»]
ProteinModelPortaliQ99JT9.
SMRiQ99JT9. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020957.

PTM databases

iPTMnetiQ99JT9.
PhosphoSiteiQ99JT9.

Proteomic databases

EPDiQ99JT9.
MaxQBiQ99JT9.
PaxDbiQ99JT9.
PeptideAtlasiQ99JT9.
PRIDEiQ99JT9.

Protocols and materials databases

DNASUi104923.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020957; ENSMUSP00000020957; ENSMUSG00000020629.
GeneIDi104923.
KEGGimmu:104923.
UCSCiuc007nfv.1. mouse.

Organism-specific databases

CTDi55256.
MGIiMGI:2144929. Adi1.

Phylogenomic databases

eggNOGiKOG2107. Eukaryota.
COG1791. LUCA.
GeneTreeiENSGT00390000008195.
HOGENOMiHOG000201071.
HOVERGENiHBG081992.
InParanoidiQ99JT9.
KOiK08967.
OMAiWIRIAVS.
OrthoDBiEOG091G0OM4.
PhylomeDBiQ99JT9.
TreeFamiTF300231.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00878.
BRENDAi1.13.11.53. 3474.
1.13.11.54. 3474.
ReactomeiR-MMU-1237112. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTraceiQ99JT9.
PROiQ99JT9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020629.
CleanExiMM_ADI1.
ExpressionAtlasiQ99JT9. baseline and differential.
GenevisibleiQ99JT9. MM.

Family and domain databases

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

Entry informationi

Entry nameiMTND_MOUSE
AccessioniPrimary (citable) accession number: Q99JT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.