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MTND_POLPP
ID   MTND_POLPP              Reviewed;         146 AA.
AC   D3BH90;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
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 {ECO:0000255|HAMAP-Rule:MF_03154}; ORFNames=PPL_07892;
OS   Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS   pallidum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC   Acytosteliaceae; Heterostelium.
OX   NCBI_TaxID=670386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26659 / Pp 5 / PN500;
RX   PubMed=21757610; DOI=10.1101/gr.121137.111;
RA   Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA   Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA   Schaap P., Gloeckner G.;
RT   "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT   origins for complex intercellular communication.";
RL   Genome Res. 21:1882-1891(2011).
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; ADBJ01000035; EFA79474.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3BH90; -.
DR   SMR; D3BH90; -.
DR   STRING; 670386.D3BH90; -.
DR   InParanoid; D3BH90; -.
DR   OMA; RGQEDEW; -.
DR   OrthoDB; 1166094at2759; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000001396; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:RHEA.
DR   GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
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..146
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000414341"
FT   BINDING         71
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         71
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         73
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         73
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         77
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         77
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         116
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         116
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   146 AA;  17568 MW;  E716C258E0169A57 CRC64;
     MKSYYFESNE PVSVQQLNNI NVLYYPMPMP DYQEKLDQIC QERGYKNRDE VKLNENTENL
     DAKLKIFFEE HLHDDEEIRF ILEGSGFFDV RDANDQWIRI RVEKGDLIIV PANMYHRFTL
     TETKQIHACR LFTDAPKWVP INRHQQ
 
 
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