ID MTND3_CAEBR Reviewed; 158 AA.
AC A8XHQ1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Acireductone dioxygenase 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD' 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Fe-ARD 3 {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) 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Ni-ARD 3 {ECO:0000255|HAMAP-Rule:MF_03154};
DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154};
GN ORFNames=CBG13458;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- CAUTION: This enzyme lacks one or more conserved metal-binding sites.
CC It may be non-functional. {ECO:0000305}.
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DR EMBL; HE600919; CAP32168.1; -; Genomic_DNA.
DR RefSeq; XP_002630079.1; XM_002630033.1.
DR AlphaFoldDB; A8XHQ1; -.
DR SMR; A8XHQ1; -.
DR STRING; 6238.A8XHQ1; -.
DR EnsemblMetazoa; CBG13458.1; CBG13458.1; WBGene00034220.
DR GeneID; 8572893; -.
DR KEGG; cbr:CBG_13458; -.
DR CTD; 8572893; -.
DR WormBase; CBG13458; CBP17805; WBGene00034220; -.
DR eggNOG; KOG2107; Eukaryota.
DR HOGENOM; CLU_090154_2_0_1; -.
DR InParanoid; A8XHQ1; -.
DR OMA; CEYGDLI; -.
DR OrthoDB; 130851at2759; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000008549; Chromosome II.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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:SF1; INACTIVE ACIREDUCTONE DIOXYGENASE 2-RELATED; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Dioxygenase; Methionine biosynthesis;
KW Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..158
FT /note="Acireductone dioxygenase 3"
FT /id="PRO_0000414339"
SQ SEQUENCE 158 AA; 18680 MW; 994252DB794FF917 CRC64;
MVQIWQMEPY PCGDPRLPHH LFPPKKITPD ELSKRTGTLY WKLDTLDQVA LAKRLTTLKL
EHNFKKEDIF TLDAETTANF DDKIEELFEE SSVPFEQARM IIEGSAYYDV EDKNGQWVRI
FCEYGDLILI PSNTCFRFTT TPKNFVKMRR FYKEEEGN
//
