ID A0A3E0L3K5_9CHRO Unreviewed; 183 AA. AC A0A3E0L3K5; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 28-JUN-2023, entry version 11. DE RecName: Full=Acireductone dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682}; DE AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682}; DE Short=DHK-MTPene dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682}; DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_01682}; DE Short=ARD' {ECO:0000256|HAMAP-Rule:MF_01682}; DE Short=Fe-ARD {ECO:0000256|HAMAP-Rule:MF_01682}; DE EC=1.13.11.54 {ECO:0000256|HAMAP-Rule:MF_01682}; DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_01682}; DE Short=ARD {ECO:0000256|HAMAP-Rule:MF_01682}; DE Short=Ni-ARD {ECO:0000256|HAMAP-Rule:MF_01682}; DE EC=1.13.11.53 {ECO:0000256|HAMAP-Rule:MF_01682}; GN Name=mtnD {ECO:0000256|HAMAP-Rule:MF_01682}; GN ORFNames=DWQ53_19210 {ECO:0000313|EMBL:REJ42098.1}; OS Microcystis flos-aquae DF17. OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Microcystaceae; Microcystis. OX NCBI_TaxID=2060470 {ECO:0000313|EMBL:REJ42098.1, ECO:0000313|Proteomes:UP000257029}; RN [1] {ECO:0000313|EMBL:REJ42098.1, ECO:0000313|Proteomes:UP000257029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF17 {ECO:0000313|EMBL:REJ42098.1}; RA Li Q., Lin F.; RT "A large-scale comparative metagenomic study reveals the eutrophication- RT driven functional interactions in six Microcystis-epibionts communities."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes 2 different reactions between oxygene 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_01682}. 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_01682}; 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|HAMAP-Rule:MF_01682}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01682}; CC Note=Binds 1 Fe(2+) cation per monomer. {ECO:0000256|HAMAP- CC Rule:MF_01682}; CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01682}; CC Note=Binds 1 nickel ion per monomer. {ECO:0000256|HAMAP-Rule:MF_01682}; 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_01682}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01682}. CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family. CC {ECO:0000256|HAMAP-Rule:MF_01682}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01682}. 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:REJ42098.1}. 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; QQWB01000036; REJ42098.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3E0L3K5; -. DR SMR; A0A3E0L3K5; -. DR EnsemblBacteria; REJ42098; REJ42098; DWQ53_19210. DR UniPathway; UPA00904; UER00878. DR Proteomes; UP000257029; Unassembled WGS sequence. 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-UniPathway. DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule. DR CDD; cd02232; cupin_ARD; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR HAMAP; MF_01682; Salvage_MtnD; 1. DR InterPro; IPR004313; ARD. DR InterPro; IPR023956; ARD_bac. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR23418:SF0; 1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE; 1. DR PANTHER; PTHR23418; 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_01682}; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP- KW Rule:MF_01682}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01682}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01682}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_01682}; KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01682}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01682}. FT BINDING 99 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 99 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 101 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 101 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 105 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 105 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 144 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT BINDING 144 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT SITE 104 FT /note="May play a role in transmitting local conformational FT changes" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" FT SITE 107 FT /note="Important to generate the dianion" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682" SQ SEQUENCE 183 AA; 20819 MW; F780422554778590 CRC64; MAILRLENGT TYTQLADISL ELAKLNVTLN YWPIENEATR QLLKQASLTD EEKEIVLTSL DGYFEQLKQE AGYQARDLIV LHPEIANLDT LLAKFERCHT HADDEVRYII DGEGVFGFVF ADGSQGELTI QPQEYINVPA HSEHWFHLTA SKRVKAVRYF TSTAGWVPEY TETVIRFPSL TAV //