MTND_DANRE
ID MTND_DANRE Reviewed; 181 AA.
AC Q6PBX5; E7FAD8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD' {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=MTCBP-1 {ECO:0000255|HAMAP-Rule:MF_03154};
GN Name=adi1; Synonyms=mtcbp1; ORFNames=zgc:73201;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the
CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
CC depending upon the metal bound in the active site. Fe-containing
CC acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-
CC methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine
CC in the methionine recycle pathway. Ni-containing acireductone
CC dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and
CC formate, and does not lie on the methionine recycle pathway.
CC {ECO:0000255|HAMAP-Rule:MF_03154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-
CC methylsulfanyl-2-oxobutanoate + formate + 2 H(+);
CC Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252;
CC EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-
CC (methylsulfanyl)propanoate + CO + formate + 2 H(+);
CC Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016,
CC ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03154};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes
CC an acireductone dioxygenase reaction producing 2-keto-4-
CC methylthiobutyrate, while nickel-binding promotes an acireductone
CC dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
CC {ECO:0000255|HAMAP-Rule:MF_03154};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 5/6. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC -!- SUBUNIT: Monomer. Interacts with MMP14. {ECO:0000255|HAMAP-
CC Rule:MF_03154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}. Cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_03154}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03154}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03154}. Note=Localizes to the plasma membrane when complexed to
CC MMP14. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC {ECO:0000255|HAMAP-Rule:MF_03154}.
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DR EMBL; CU634006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059549; AAH59549.1; -; mRNA.
DR RefSeq; NP_001232841.1; NM_001245912.1.
DR RefSeq; NP_955962.1; NM_199668.1.
DR AlphaFoldDB; Q6PBX5; -.
DR SMR; Q6PBX5; -.
DR STRING; 7955.ENSDARP00000025996; -.
DR PaxDb; Q6PBX5; -.
DR Ensembl; ENSDART00000025229; ENSDARP00000025996; ENSDARG00000020448.
DR GeneID; 324079; -.
DR KEGG; dre:324079; -.
DR CTD; 55256; -.
DR ZFIN; ZDB-GENE-030131-2799; adi1.
DR eggNOG; KOG2107; Eukaryota.
DR GeneTree; ENSGT00390000008195; -.
DR HOGENOM; CLU_090154_0_1_1; -.
DR InParanoid; Q6PBX5; -.
DR OMA; RGQEDEW; -.
DR OrthoDB; 1166094at2759; -.
DR PhylomeDB; Q6PBX5; -.
DR TreeFam; TF300231; -.
DR Reactome; R-DRE-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00878.
DR PRO; PR:Q6PBX5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000020448; Expressed in intestine and 36 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:RHEA.
DR GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB.
DR GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central.
DR CDD; cd02232; cupin_ARD; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_03154; Salvage_MtnD_euk; 1.
DR InterPro; IPR004313; ARD.
DR InterPro; IPR027496; ARD_euk.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR23418; PTHR23418; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cell membrane; Cytoplasm; Dioxygenase; Iron;
KW Membrane; Metal-binding; Methionine biosynthesis; Nickel; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..181
FT /note="Acireductone dioxygenase"
FT /id="PRO_0000223188"
FT BINDING 91
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 91
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 93
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 93
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 97
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 97
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 136
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT CONFLICT 179
FT /note="G -> R (in Ref. 2; AAH59549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 21423 MW; 5504349AF2F77D46 CRC64;
MSVFEAWYMD EESGEDQRLP HKLSPNQPVS VQQLEHIGVF HWKLNADIYE NDPELQKIRE
EKGYSFMDII TIHPDKLPDY QNKLKMFYEE HLHLDDEIRY ILEGSSYFDV RDEGDRWIRI
AVSKGDLITL PAGIYHRFTV DESNYTKAMR LFVGEPVWKA YNRPADDFDI RKEYVNSLGS
S
