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MTND_DICDI
ID   MTND_DICDI              Reviewed;         147 AA.
AC   Q54ER6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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};
GN   Name=adi1; ORFNames=DDB_G0291376;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}.
CC       Nucleus {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; AAFI02000177; EAL61672.1; -; Genomic_DNA.
DR   RefSeq; XP_635174.1; XM_630082.1.
DR   AlphaFoldDB; Q54ER6; -.
DR   SMR; Q54ER6; -.
DR   STRING; 44689.DDB0230998; -.
DR   PaxDb; Q54ER6; -.
DR   EnsemblProtists; EAL61672; EAL61672; DDB_G0291376.
DR   GeneID; 8628120; -.
DR   KEGG; ddi:DDB_G0291376; -.
DR   dictyBase; DDB_G0291376; adi1.
DR   eggNOG; KOG2107; Eukaryota.
DR   HOGENOM; CLU_090154_1_1_1; -.
DR   InParanoid; Q54ER6; -.
DR   OMA; RGQEDEW; -.
DR   PhylomeDB; Q54ER6; -.
DR   Reactome; R-DDI-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00878.
DR   PRO; PR:Q54ER6; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR   GO; GO:0005634; C:nucleus; ISS:dictyBase.
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:dictyBase.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:dictyBase.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nickel; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..147
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000328196"
FT   BINDING         74
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         74
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         76
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         76
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         80
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         80
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         119
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         119
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"
SQ   SEQUENCE   147 AA;  17815 MW;  EFD51F99E932E344 CRC64;
     MKSYFYDNES DVISLDYLKE HNVLYFPMDR EKENYKEPLE TLCKERGYKN RDEVKLSKET
     PGLEDKLKIF FEEHLHDDEE IRFILDGCGF FDIRDKNDKW VKIKEKKGDL IIVPANMYHR
     FALDESRNIH AMRLFTDAPK WVPINRY
 
 
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