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Protein

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

Gene

ADI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.UniRule annotation2 Publications

Catalytic activityi

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate.UniRule annotation1 Publication

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per monomer (Ref.14). 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), Methylthioribose-1-phosphate isomerase (mtnA)
  2. Methylthioribulose-1-phosphate dehydratase (APIP), 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)
  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)DescriptionActionsGraphical viewLength
Metal bindingi88Iron or nickelUniRule annotation1 Publication1
Metal bindingi90Iron or nickelUniRule annotation1 Publication1
Metal bindingi94Iron or nickelUniRule annotation1 Publication1
Metal bindingi133Iron or nickelUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

  • L-methionine salvage from methylthioadenosine Source: UniProtKB

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-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
Submergence-induced protein-like factor
Short name:
Sip-L
Gene namesi
Name:ADI1UniRule annotation
Synonyms:MTCBP1UniRule annotation
ORF Names:HMFT1638
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000182551.13
HGNCiHGNC:30576 ADI1
MIMi613400 gene
neXtProtiNX_Q9BV57

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94E → A: Loss of aci-reductone dioxygenase activity. 1 Publication1

Organism-specific databases

DisGeNETi55256
OpenTargetsiENSG00000182551
PharmGKBiPA143485291

Chemistry databases

ChEMBLiCHEMBL3817720
DrugBankiDB02325 Isopropyl Alcohol

Polymorphism and mutation databases

BioMutaiADI1
DMDMi74733289

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001629421 – 1791,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseAdd BLAST179

Proteomic databases

EPDiQ9BV57
MaxQBiQ9BV57
PaxDbiQ9BV57
PeptideAtlasiQ9BV57
PRIDEiQ9BV57
ProteomicsDBi79171
79172 [Q9BV57-2]
TopDownProteomicsiQ9BV57-1 [Q9BV57-1]
Q9BV57-2 [Q9BV57-2]

PTM databases

iPTMnetiQ9BV57
PhosphoSitePlusiQ9BV57

Expressioni

Tissue specificityi

Detected in heart, colon, lung, stomach, brain, spleen, liver, skeletal muscle and kidney.2 Publications

Gene expression databases

BgeeiENSG00000182551
CleanExiHS_ADI1
ExpressionAtlasiQ9BV57 baseline and differential
GenevisibleiQ9BV57 HS

Organism-specific databases

HPAiHPA035403
HPA035404

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with MMP14.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MMP14P502814EBI-992807,EBI-992788

Protein-protein interaction databases

BioGridi120547, 18 interactors
IntActiQ9BV57, 5 interactors
STRINGi9606.ENSP00000333666

Structurei

Secondary structure

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi14 – 16Combined sources3
Helixi28 – 32Combined sources5
Turni33 – 35Combined sources3
Beta strandi37 – 40Combined sources4
Beta strandi43 – 45Combined sources3
Helixi46 – 48Combined sources3
Helixi50 – 58Combined sources9
Beta strandi63 – 70Combined sources8
Turni71 – 73Combined sources3
Helixi77 – 85Combined sources9
Beta strandi94 – 101Combined sources8
Beta strandi103 – 108Combined sources6
Beta strandi114 – 119Combined sources6
Beta strandi123 – 127Combined sources5
Beta strandi133 – 137Combined sources5
Beta strandi143 – 152Combined sources10
Beta strandi158 – 160Combined sources3
Helixi166 – 176Combined sources11

3D structure databases

ProteinModelPortaliQ9BV57
SMRiQ9BV57
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2107 Eukaryota
COG1791 LUCA
GeneTreeiENSGT00390000008195
HOVERGENiHBG081992
InParanoidiQ9BV57
KOiK08967
OMAiKERNYSW
OrthoDBiEOG091G0OM4
PhylomeDBiQ9BV57
TreeFamiTF300231

Family and domain databases

Gene3Di2.60.120.10, 1 hit
HAMAPiMF_03154 Salvage_MtnD_euk, 1 hit
InterProiView protein in InterPro
IPR004313 ARD
IPR027496 ARD_euk
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf
PANTHERiPTHR23418 PTHR23418, 1 hit
PfamiView protein in Pfam
PF03079 ARD, 1 hit
SUPFAMiSSF51182 SSF51182, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BV57-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVQAWYMDDA PGDPRQPHRP DPGRPVGLEQ LRRLGVLYWK LDADKYENDP
60 70 80 90 100
ELEKIRRERN YSWMDIITIC KDKLPNYEEK IKMFYEEHLH LDDEIRYILD
110 120 130 140 150
GSGYFDVRDK EDQWIRIFME KGDMVTLPAG IYHRFTVDEK NYTKAMRLFV
160 170
GEPVWTAYNR PADHFEARGQ YVKFLAQTA
Length:179
Mass (Da):21,498
Last modified:June 1, 2001 - v1
Checksum:i92E13B9718D44C27
GO
Isoform 2 (identifier: Q9BV57-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MVQAWYMDDAPGDPRQPHRPDPGRPVGLEQLRRLGVLYWK → MSVKSSKLMFLCHGSSRSLHSGSLTSCNTGVCCS

Note: No experimental confirmation available.
Show »
Length:173
Mass (Da):20,332
Checksum:i5AE5570210391A36
GO

Sequence cautioni

The sequence AAL25800 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD38646 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD96187 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3Q → L in BAA91901 (PubMed:14702039).Curated1
Sequence conflicti108R → G in BAD96187 (Ref. 5) Curated1
Sequence conflicti170Q → K in AAP97173 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0158221 – 40MVQAW…VLYWK → MSVKSSKLMFLCHGSSRSLH SGSLTSCNTGVCCS in isoform 2. 1 PublicationAdd BLAST40

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB158319 mRNA Translation: BAD10866.1
AF087863 mRNA Translation: AAP97173.1
AB073609 mRNA Translation: BAD38646.1 Different initiation.
AK001775 mRNA Translation: BAA91901.1
AK127473 mRNA Translation: BAC86996.1
AK222467 mRNA Translation: BAD96187.1 Different initiation.
AC142528 Genomic DNA Translation: AAX82038.1
AC114810 Genomic DNA Translation: AAY24022.1
CH471053 Genomic DNA Translation: EAX01064.1
CH471053 Genomic DNA Translation: EAX01065.1
BC001467 mRNA Translation: AAH01467.1
AF403478 mRNA Translation: AAL25800.1 Different initiation.
CCDSiCCDS1653.1 [Q9BV57-1]
CCDS77380.1 [Q9BV57-2]
RefSeqiNP_001293006.1, NM_001306077.1 [Q9BV57-2]
NP_060739.2, NM_018269.3 [Q9BV57-1]
UniGeneiHs.502773

Genome annotation databases

EnsembliENST00000327435; ENSP00000333666; ENSG00000182551 [Q9BV57-1]
ENST00000382093; ENSP00000371525; ENSG00000182551 [Q9BV57-2]
GeneIDi55256
KEGGihsa:55256
UCSCiuc002qxp.5 human [Q9BV57-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiMTND_HUMAN
AccessioniPrimary (citable) accession number: Q9BV57
Secondary accession number(s): D6W4Y3
, Q53HW3, Q53QD3, Q57YV7, Q68CK2, Q6ZSF7, Q7Z512, Q96P85, Q9NV57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 1, 2001
Last modified: July 18, 2018
This is version 157 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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