ID MTND2_PHYPA Reviewed; 195 AA. AC A9SS00; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Acireductone dioxygenase 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=ARD' 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=Fe-ARD 2 {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) 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=ARD 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=Ni-ARD 2 {ECO:0000255|HAMAP-Rule:MF_03154}; DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154}; GN ORFNames=PHYPADRAFT_134384; OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium. OX NCBI_TaxID=3218; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y., RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the conquest RT of land by plants."; RL Science 319:64-69(2008). 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03154}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000255|HAMAP- CC 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 --------------------------------------------------------------------------- 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; DS545000; EDQ66042.1; -; Genomic_DNA. DR RefSeq; XP_001769170.1; XM_001769118.1. DR AlphaFoldDB; A9SS00; -. DR PaxDb; 3218-PP1S111_19V6-1; -. DR eggNOG; KOG2107; Eukaryota. DR HOGENOM; CLU_090154_0_1_1; -. DR InParanoid; A9SS00; -. DR UniPathway; UPA00904; UER00878. DR Proteomes; UP000006727; Unplaced. 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; IBA:GO_Central. 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 GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central. 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; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Methionine biosynthesis; Nickel; Nucleus; Oxidoreductase; KW Reference proteome. FT CHAIN 1..195 FT /note="Acireductone dioxygenase 2" FT /id="PRO_0000414343" FT BINDING 94 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 94 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 96 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 96 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 100 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 100 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 139 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 139 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 195 AA; 23199 MW; D0AED4C8E9A82C70 CRC64; MQVQRPPLEA WYMNDSEEDQ RLPHHRNPPE YVTLEKLAAL GVIHWVLDAD NHETDPELSI IRKDRGYNYT DVITVCPEML PSYEAKIKSF YEEHIHMDEE IRYCLDGSGY FDVRDPEDHW IRIWVRKGDM IVLPAGCYHR FTLDEHNYIM AMRLFVGEPI WTPYNRPQDE HPVRKGYVHQ FLQPELLDVD MSISA //