ID   MTND2_CAEBR             Reviewed;         159 AA.
AC   A8X409;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable inactive acireductone dioxygenase 2 {ECO:0000255|HAMAP-Rule:MF_03154};
GN   ORFNames=CBG06970;
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: Probable inactive acireductone dioxygenase.
CC       {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; HE600960; CAP27369.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X409; -.
DR   SMR; A8X409; -.
DR   STRING; 6238.CBG06970; -.
DR   EnsemblMetazoa; CBG06970.1; CBG06970.1; WBGene00029150.
DR   WormBase; CBG06970; CBP25336; WBGene00029150; -.
DR   eggNOG; KOG2107; Eukaryota.
DR   HOGENOM; CLU_090154_2_0_1; -.
DR   InParanoid; A8X409; -.
DR   OMA; TGVVYYK; -.
DR   OrthoDB; 1166094at2759; -.
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:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
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   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..159
FT                   /note="Probable inactive acireductone dioxygenase 2"
FT                   /id="PRO_0000414338"
SQ   SEQUENCE   159 AA;  18414 MW;  E8A2F858C7CCE699 CRC64;
     MQIWHMEPFP CGDRRLPHHV FPPKKITTTQ LGALAGVQYY KVDLEDTASM KKRLSAVKTE
     KNVTFTDVFT VSETMLDFDD KMEQFYEAQT QKEDVISLVV EGTCYYDVEP EDDSWIRVQL
     EKGDLIVIPK GLSHRFTTTP QNFVKIQRFF SRKVEGTQG