ADI1_USTMD
ID ADI1_USTMD Reviewed; 443 AA.
AC A0A0U2X0E4;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Aconitate-delta-isomerase 1 {ECO:0000303|PubMed:26639528};
DE EC=5.-.-.- {ECO:0000269|PubMed:26639528};
DE AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein ADI1 {ECO:0000305};
GN Name=ADI1 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_11778;
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, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND PATHWAY.
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.
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: Aconitate-delta-isomerase; part of the gene cluster that
CC mediates the biosynthesis of itaconic acid and 2-hydroxyparaconate
CC (PubMed:26639528, PubMed:27750034). Cis-aconitate is secreted by the
CC mitochondrial tricarboxylate transporter MTT1. In the cytosol cis-
CC aconitate is converted into trans-aconitate via isomerization by the
CC aconitate-delta-isomerase ADI1 (PubMed:26639528). Decarboxylation of
CC trans-aconitate by the trans-aconitate decarboxylase TAD1 then leads
CC then to the production of itaconic acid (PubMed:26639528). The
CC cytochrome P450 monooxygenase CYP3 further converts itaconate to 2-
CC hydroxyparaconate via oxidation of the double bond, leading to a
CC transient epoxide, which can subsequently be lactonized to produce 2-
CC hydroxyparaconate (PubMed:27750034). Secretion of itaconate and
CC possibly 2-hydroxyparaconate into the medium is mediated by the major
CC facilitator ITP1 (PubMed:26639528, PubMed:27750034). The glyoxalase
CC domain-containing protein RDO1 is not involved in the biosynthesis of
CC itaconate and 2-hydroxyparaconate, however, it might play a role in the
CC further conversion of 2-hydroxyparaconate to itatartarate
CC (PubMed:27750034). {ECO:0000269|PubMed:26639528,
CC ECO:0000269|PubMed:27750034}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26639528}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26639528}.
CC Nucleus {ECO:0000269|PubMed:26639528}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of itaconic acid
CC (PubMed:26639528). {ECO:0000269|PubMed:26639528}.
CC -!- SIMILARITY: Belongs to the PrpF family. {ECO:0000305}.
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DR EMBL; KT852988; ALS30798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2X0E4; -.
DR SMR; A0A0U2X0E4; -.
DR VEuPathDB; FungiDB:UMAG_11778; -.
DR BioCyc; MetaCyc:MON-20620; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR007400; PrpF_protein.
DR PANTHER; PTHR43709; PTHR43709; 1.
DR Pfam; PF04303; PrpF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Nucleus.
FT CHAIN 1..443
FT /note="Aconitate-delta-isomerase 1"
FT /id="PRO_0000438675"
SQ SEQUENCE 443 AA; 47285 MW; 680F1201A5540453 CRC64;
MLHPIDTTIY RAGTSRGLYF LASDLPAEPS ERDAALISIM GSGHPLQIDG MGGGNSLTSK
VAIVSASTQR SEFDVDYLFC QVGITERFVD TAPNCGNLMS GVAAFAIERG LVQPHPSDTT
CLVRIFNLNS RQASELVIPV YNGRVHYDDI DDMHMQRPSA RVGLRFLDTV GSCTGKLLPT
GNASDWIDGL KVSIIDSAVP VVFIRQHDVG ITGSEAPATL NANTALLDRL ERVRLEAGRR
MGLGDVSGSV VPKLSLIGPG TETTTFTARY FTPKACHNAH AVTGAICTAG AAYIDGSVVC
EILSSRASAC SASQRRISIE HPSGVLEVGL VPPENAAQSL VDVAVVERSV ALIAHARVYY
TTPDRRRSYD SPLTSPSTPA DTHNLFDAAY RPVIQPSDTD VEAPHMLALE NKEQCVSRCD
TALHHIVASY GASDAHASDR SLS