ID   TAD1_USTMD              Reviewed;         493 AA.
AC   A0A0U2UYC4;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Trans-aconitate decarboxylase 1 {ECO:0000303|PubMed:26639528};
DE            EC=4.1.1.113 {ECO:0000269|PubMed:26639528};
DE   AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein TAD1 {ECO:0000305};
GN   Name=TAD1 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_05076;
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: Trans-aconitate decarboxylase; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + trans-aconitate = CO2 + itaconate;
CC         Xref=Rhea:RHEA:57728, ChEBI:CHEBI:15378, ChEBI:CHEBI:15708,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17240; EC=4.1.1.113;
CC         Evidence={ECO:0000269|PubMed:26639528};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57729;
CC         Evidence={ECO:0000269|PubMed:26639528};
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 class-II fumarase/aspartase family.
CC       {ECO:0000305}.
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DR   EMBL; KT852988; ALS30796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U2UYC4; -.
DR   SMR; A0A0U2UYC4; -.
DR   VEuPathDB; FungiDB:UMAG_05076; -.
DR   OMA; NTPNIGW; -.
DR   BioCyc; MetaCyc:MON-20618; -.
DR   BRENDA; 4.1.1.113; 6587.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Nucleus.
FT   CHAIN           1..493
FT                   /note="Trans-aconitate decarboxylase 1"
FT                   /id="PRO_0000438676"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  53972 MW;  F0CC2DF2F7E1C61C CRC64;
     MAPALNANPT TKRDELSAPS ASHKLGMSSM ASRAAGGGLK LTGLPDLSDS AGTLSDIFGT
     PQMREIWSDQ NRVACYLEIE AALAIVQADL GIIPKNAAHE IVEHCRVQEI DWALYKQKTE
     LIGYPVLGIV QQLVANCKDG LGEYCHWGAT TQDITDTATV MQIRQSLTLV KQRLDSIVSS
     LEHLAEQHRN VPMAARSNLK QAVPITFGFK MARFLATFRR HQQRLVELEK RVYTLEFGGA
     AGNLSSLGDQ GIATHDALAK MLDLAPAEIA WHTEHDRFAE VGTFLGLLTG TLAKLATDIK
     LMSQTEVGEV GEPFISNRGS SSTMPQKNNP ISCVYIHACA ANVRQGAAAL LDAMQSDHER
     GTGPWEIIWV QLPLMMNWTS AALNNADFVL RGLQVFPDAM QHNLDLSKGL IVSEAVMMGL
     GNTLGRQYAH DAVYECCRTA FVQDRPLLDV LLENHEIASK LDRTELEKLC DPANYLGQCS
     QWIDRVLSRP SSA