CYP3_USTMD
ID CYP3_USTMD Reviewed; 540 AA.
AC A0A0U2V7I8;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cytochrome P450 monooxygenase CYP3 {ECO:0000303|PubMed:27750034};
DE EC=1.-.-.- {ECO:0000269|PubMed:27750034};
DE AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein CYP3 {ECO:0000305};
GN Name=CYP3 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_05074;
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, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Cytochrome P450 monooxygenase; 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27750034}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the itaconic acid production
CC (PubMed:26639528). Abolishes completely the production of 2-
CC hydroxyparaconate (PubMed:27750034). {ECO:0000269|PubMed:26639528,
CC ECO:0000269|PubMed:27750034}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KT852988; ALS30800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2V7I8; -.
DR SMR; A0A0U2V7I8; -.
DR VEuPathDB; FungiDB:UMAG_05074; -.
DR OMA; RRRTEYH; -.
DR BioCyc; MetaCyc:MON-20619; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="Cytochrome P450 monooxygenase CYP3"
FT /id="PRO_0000438677"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 471
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 540 AA; 60000 MW; C5AE399AA4953C82 CRC64;
MNTTKLLGTG ALSPSFVFDH DSGNAIFGLS SSTLVVLVAM IAVSTLTLKS VLPGDRSINL
PGPRGWPIVG SWFDLGNNWA EYFRQAAKEY GDVFKVHIGN RTVVVVNSPK AAHILFNEHG
SSLISRPWFY TFHGVLSKSS AFTIGTSAWS DSTKNKRKAA ATALNRPAVQ SYMPIIVEES
LDAVRRILND GNAGKNGIVP YSYFQRLALN TSFQVNYGFR MGERDDGLFD EISEVIAKVA
SVRAVTGSLQ DYVPLMRYLP ANAKSKAAAS YGLRRKKFMS KLYEELEQRV NQGKDESCIT
GNILKDTESR KKLSRLEIDS ICLSMVSAGL DTFANTMIWT IGFLAKHPEI QRKAQAELLA
HYPNRELPHV DSEDLVYIHA MAKEASRLFN VFRICLPRTN VSDVTYNNAV IPAGTTFFLN
SWACNVDAEK FADPFEFKPE RFMDKSASNA HVENKMGGVE TYAFGMGRRM CPGVFLALRE
IYTTLVFLTH FFDIAPDGEY DIDPLTAVED GRAFSVRPKP FKVRCTPRPG VDLSPVLDKQ
