MTND_ASPFU
ID MTND_ASPFU Reviewed; 176 AA.
AC Q4WDE1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 100.
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=AFUA_6G04430;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL85597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000012; EAL85597.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_747635.1; XM_742542.1.
DR AlphaFoldDB; Q4WDE1; -.
DR SMR; Q4WDE1; -.
DR STRING; 746128.CADAFUBP00009123; -.
DR GeneID; 3505296; -.
DR KEGG; afm:AFUA_6G04430; -.
DR eggNOG; KOG2107; Eukaryota.
DR HOGENOM; CLU_090154_0_0_1; -.
DR InParanoid; Q4WDE1; -.
DR OrthoDB; 1166094at2759; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000002530; Chromosome 6.
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; IBA:GO_Central.
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 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..176
FT /note="Acireductone dioxygenase"
FT /id="PRO_0000414362"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03154"
SQ SEQUENCE 176 AA; 20848 MW; 88B020A256BABBB8 CRC64;
MKAYWYDNKP GDQREPHDSG RPVTVDYLAS IGVQYYHFPS LESVNELAKE RGYKNRDEIV
VSPQAMGDVY EEKVKMFFNE HLHEDEEIRY IRDGEGYFDV RGQEDEWVRI KLAKDDLIIL
PAGIYHRFTT DDKNYVKAMR LFQEEPKWTP LNRGPDVDEN SHRQSYLRTI QNKTVA
