IED ID | IndEnz0002007550 |
Enzyme Type ID | protease007550 |
Protein Name |
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase EC 1.13.11.54 Acireductone dioxygenase Fe 2+ -requiring ARD Fe-ARD Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1 MTCBP-1 Submergence-induced protein-like factor Sip-L |
Gene Name | ADI1 MTCBP1 HMFT1638 |
Organism | Homo sapiens (Human) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MVQAWYMDDAPGDPRQPHRPDPGRPVGLEQLRRLGVLYWKLDADKYENDPELEKIRRERNYSWMDIITICKDKLPNYEEKIKMFYEEHLHLDDEIRYILDGSGYFDVRDKEDQWIRIFMEKGDMVTLPAGIYHRFTVDEKNYTKAMRLFVGEPVWTAYNRPADHFEARGQYVKFLAQTA |
Enzyme Length | 179 |
Uniprot Accession Number | Q9BV57 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+); Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252; EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:15938715}; |
DNA Binding | |
EC Number | 1.13.11.54 |
Enzyme Function | FUNCTION: 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. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line. {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:15938715}. |
Temperature Dependency | |
PH Dependency | |
Pathway | 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. {ECO:0000255|HAMAP-Rule:MF_03154}. |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (12); Chain (1); Compositional bias (1); Erroneous initiation (3); Helix (5); Metal binding (4); Mutagenesis (1); Region (1); Sequence conflict (3); Turn (2) |
Keywords | 3D-structure;Alternative splicing;Amino-acid biosynthesis;Cell membrane;Cytoplasm;Dioxygenase;Direct protein sequencing;Iron;Membrane;Metal-binding;Methionine biosynthesis;Nucleus;Oxidoreductase;Reference proteome |
Interact With | Q9UKG1; P50281 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the plasma membrane when complexed to MMP14. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | NMR spectroscopy (1); X-ray crystallography (1) |
Cross Reference PDB | 4QGN; 7JXG; |
Mapped Pubmed ID | 17212658; 17353931; 17786183; 19626614; 20379614; 23602568; 25640948; 26537061; 28062648; 30066900; 30487181; 32480040; 33135413; |
Motif | |
Gene Encoded By | |
Mass | 21,498 |
Kinetics | |
Metal Binding | METAL 88; /note="Iron or nickel"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|Ref.14"; METAL 90; /note="Iron or nickel"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|Ref.14"; METAL 94; /note="Iron or nickel"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|Ref.14"; METAL 133; /note="Iron or nickel"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|Ref.14" |
Rhea ID | RHEA:24504 |
Cross Reference Brenda | 1.13.11.53;1.13.11.54; |