ID F7W354_SORMK Unreviewed; 157 AA.
AC F7W354;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Acireductone dioxygenase {ECO:0000256|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=ARD' {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=Fe-ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE EC=1.13.11.54 {ECO:0000256|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=Ni-ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE EC=1.13.11.53 {ECO:0000256|HAMAP-Rule:MF_03154};
GN Name=ADI1 {ECO:0000256|HAMAP-Rule:MF_03154};
GN ORFNames=SMAC_02277 {ECO:0000313|EMBL:CCC12056.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12056.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12056.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12056.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:0000256|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:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000428,
CC ECO:0000256|HAMAP-Rule:MF_03154};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03154};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03154}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03154}.
CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC {ECO:0000256|HAMAP-Rule:MF_03154}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCC12056.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABT02000023; CCC12056.1; -; Genomic_DNA.
DR RefSeq; XP_003350564.1; XM_003350516.1.
DR AlphaFoldDB; F7W354; -.
DR STRING; 771870.F7W354; -.
DR GeneID; 10808112; -.
DR KEGG; smp:SMAC_02277; -.
DR VEuPathDB; FungiDB:SMAC_02277; -.
DR eggNOG; KOG2107; Eukaryota.
DR HOGENOM; CLU_090154_1_0_1; -.
DR InParanoid; F7W354; -.
DR OMA; MVRAWYM; -.
DR OrthoDB; 130851at2759; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000001881; 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:UniProtKB-UniRule.
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:0016151; F:nickel cation 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; Jelly Rolls; 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; ACIREDUCTONE DIOXYGENASE; 1.
DR PANTHER; PTHR23418:SF0; ACIREDUCTONE DIOXYGENASE; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03154};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03154};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_03154};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03154};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03154}; Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT BINDING 81
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 81
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 83
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 83
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 87
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 87
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 126
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 126
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
SQ SEQUENCE 157 AA; 18398 MW; B4CD711831754CF8 CRC64;
MKAYFYDNLP GDQRLPHDSG REVTVSDLEK VGVLYFRIPE LEGVNALASE RGYKNRDEIT
ISPEKMGAIY ETKVKQFFDE HLHEDEEIRY IRDGAGYFDV RNEGDEWIRI KLVKDDLIIL
PAGIYHRFTT DDTDYIQAMR LFKEEPQVDA SQPHRRA
//
