ID   RDO1_USTMD              Reviewed;         176 AA.
AC   A0A0U2WCB2;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Glyoxalase domain-containing protein RDO1 {ECO:0000305};
DE   AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein RDO1 {ECO:0000305};
DE   AltName: Full=Putative ring-cleaving dioxygenase 1 {ECO:0000303|PubMed:26639528};
GN   Name=RDO1 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_12299;
OS   Ustilago maydis (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MB215;
RX   PubMed=26639528; DOI=10.1111/1751-7915.12329;
RA   Geiser E., Przybilla S.K., Friedrich A., Buckel W., Wierckx N., Blank L.M.,
RA   Boelker M.;
RT   "Ustilago maydis produces itaconic acid via the unusual intermediate trans-
RT   aconitate.";
RL   Microb. Biotechnol. 9:116-126(2016).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27750034; DOI=10.1016/j.ymben.2016.10.006;
RA   Geiser E., Przybilla S.K., Engel M., Kleineberg W., Buettner L.,
RA   Sarikaya E., Hartog T.D., Klankermayer J., Leitner W., Boelker M.,
RA   Blank L.M., Wierckx N.;
RT   "Genetic and biochemical insights into the itaconate pathway of Ustilago
RT   maydis enable enhanced production.";
RL   Metab. Eng. 38:427-435(2016).
CC   -!- FUNCTION: Glyoxalase domain-containing protein; part of the gene
CC       cluster that mediates the biosynthesis of itaconic acid and 2-
CC       hydroxyparaconate (PubMed:26639528, PubMed:27750034). Cis-aconitate is
CC       secreted by the mitochondrial tricarboxylate transporter MTT1. In the
CC       cytosol cis-aconitate is converted into trans-aconitate via
CC       isomerization by the aconitate-delta-isomerase ADI1 (PubMed:26639528).
CC       Decarboxylation of trans-aconitate by the trans-aconitate decarboxylase
CC       TAD1 then leads then to the production of itaconic acid
CC       (PubMed:26639528). The cytochrome P450 monooxygenase CYP3 further
CC       converts itaconate to 2-hydroxyparaconate via oxidation of the double
CC       bond, leading to a transient epoxide, which can subsequently be
CC       lactonized to produce 2-hydroxyparaconate (PubMed:27750034). Secretion
CC       of itaconate and possibly 2-hydroxyparaconate into the medium is
CC       mediated by the major facilitator ITP1 (PubMed:26639528,
CC       PubMed:27750034). The glyoxalase domain-containing protein RDO1 is not
CC       involved in the biosynthesis of itaconate and 2-hydroxyparaconate,
CC       however, it might play a role in the further conversion of 2-
CC       hydroxyparaconate to itatartarate (PubMed:27750034).
CC       {ECO:0000269|PubMed:26639528, ECO:0000269|PubMed:27750034}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:27750034}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect the itaconic acid nor 2-
CC       hydroxyparaconate production (PubMed:26639528, PubMed:27750034).
CC       {ECO:0000269|PubMed:26639528, ECO:0000269|PubMed:27750034}.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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; KT852988; ALS30794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U2WCB2; -.
DR   SMR; A0A0U2WCB2; -.
DR   VEuPathDB; FungiDB:UMAG_12299; -.
DR   BioCyc; MetaCyc:MON-20622; -.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..176
FT                   /note="Glyoxalase domain-containing protein RDO1"
FT                   /id="PRO_0000438679"
SQ   SEQUENCE   176 AA;  19721 MW;  3CA1DA09FE7AA01C CRC64;
     MLRSSQARSV VRSSQWATTA RVHQLELPSG WKPSALGVAP WQQRQQRQLS VRSLDHLVIT
     CHDMDKTIDF YTRLGMSVVQ FGQGRKALEF GSQKINLHQK GKEFEPKALV PQPGSQDLCF
     VIHDSIADAQ KHLQEHGIQV VEGPVKRTGA VGPILSIYVR DPDNNLIELS SYQDAK