CMU1_USTMA
ID CMU1_USTMA Reviewed; 290 AA.
AC A0A0D1DWQ2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Secreted chorismate mutase {ECO:0000303|PubMed:21976020};
DE EC=5.4.99.5 {ECO:0000269|PubMed:21976020};
DE Flags: Precursor;
GN Name=CMU1; ORFNames=UMAG_05731;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RX PubMed=20360107; DOI=10.1126/science.1185775;
RA Skibbe D.S., Doehlemann G., Fernandes J., Walbot V.;
RT "Maize tumors caused by Ustilago maydis require organ-specific genes in
RT host and pathogen.";
RL Science 328:89-92(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DISRUPTION PHENOTYPE, SUBUNIT, MUTAGENESIS OF ARG-183 AND
RP LYS-194, AND INTERACTION WITH HOST CYTOSOLIC CM2.
RX PubMed=21976020; DOI=10.1038/nature10454;
RA Djamei A., Schipper K., Rabe F., Ghosh A., Vincon V., Kahnt J., Osorio S.,
RA Tohge T., Fernie A.R., Feussner I., Feussner K., Meinicke P.,
RA Stierhof Y.D., Schwarz H., Macek B., Mann M., Kahmann R.;
RT "Metabolic priming by a secreted fungal effector.";
RL Nature 478:395-398(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-290 IN COMPLEX WITH HOST KWL1,
RP SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS OF 1-MET--ALA-21 AND
RP 117-VAL--ARG-140.
RX PubMed=30651637; DOI=10.1038/s41586-018-0857-9;
RA Han X., Altegoer F., Steinchen W., Binnebesel L., Schuhmacher J.,
RA Glatter T., Giammarinaro P.I., Djamei A., Rensing S.A., Reissmann S.,
RA Kahmann R., Bange G.;
RT "A kiwellin disarms the metabolic activity of a secreted fungal virulence
RT factor.";
RL Nature 565:650-653(2019).
CC -!- FUNCTION: Secreted chorismate mutase that is one component of a
CC cocktail of effectors shaping the host metabolome and acting as
CC virulence factors. The enzyme is taken up by plant cells, can spread to
CC neighboring cells where it affects the biosynthesis of the plant immune
CC signal salicylic acid by channelling chorismate into the
CC phenylpropanoid pathway (PubMed:21976020, PubMed:30651637). Interfers
CC with the activity of host cytosolic chorismate mutase CM2 through
CC heterodimerization (PubMed:21976020). {ECO:0000269|PubMed:21976020,
CC ECO:0000269|PubMed:30651637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637};
CC -!- ACTIVITY REGULATION: Contrary to classical chorismate mutases, CMU1 is
CC not subject to allosteric regulation by tryptophan and tyrosine
CC (PubMed:21976020, PubMed:30651637). Activity is decreased in a non-
CC competitive and allosteric manner by the binding of the host defense
CC kiwellin KWL1 which probably blocks substrate access to the active site
CC of CMU1 (PubMed:30651637). {ECO:0000269|PubMed:21976020,
CC ECO:0000269|PubMed:30651637}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for chorismate {ECO:0000269|PubMed:30651637};
CC Vmax=40.8 umol/min/mg enzyme {ECO:0000269|PubMed:30651637};
CC Vmax=21.1 umol/min/mg enzyme (when bound to host KWL1)
CC {ECO:0000269|PubMed:30651637};
CC -!- SUBUNIT: Homodimer (PubMed:21976020, PubMed:30651637). Forms a
CC heterodimer with the host cytosolic chorismate mutase CM2
CC (PubMed:21976020). Interacts with the host kiwellin KWL1 which acts as
CC a defense protein that protects maize from infection (PubMed:30651637).
CC {ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21976020}. Host
CC cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is
CC translocated to host plant cells and spreads to neighboring tissue. The
CC spreading is likely to occur through plasmodesmata.
CC {ECO:0000269|PubMed:21976020}.
CC -!- INDUCTION: Expression is specifically up-regulated during biotrophic
CC development (PubMed:21976020). CMU1 is one of the most highly expressed
CC fungal genes during plant colonization (PubMed:20360107).
CC {ECO:0000269|PubMed:20360107, ECO:0000269|PubMed:21976020}.
CC -!- DOMAIN: The extensive loop region (ELR) is specific for fungal secreted
CC chorismate mutases and is required for the interaction with the host
CC defense kiwellin KWL1. {ECO:0000269|PubMed:30651637}.
CC -!- DISRUPTION PHENOTYPE: Decreases significantly the amount of tumors
CC produced during host maize infection. {ECO:0000269|PubMed:21976020}.
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DR EMBL; CM003155; KIS66950.1; -; Genomic_DNA.
DR RefSeq; XP_011391476.1; XM_011393174.1.
DR PDB; 6FPF; X-ray; 2.20 A; A/C/D/E=22-290.
DR PDB; 6FPG; X-ray; 1.80 A; B/C/F/G=22-290.
DR PDB; 6TI2; X-ray; 2.75 A; B/C=22-290.
DR PDBsum; 6FPF; -.
DR PDBsum; 6FPG; -.
DR PDBsum; 6TI2; -.
DR AlphaFoldDB; A0A0D1DWQ2; -.
DR SMR; A0A0D1DWQ2; -.
DR EnsemblFungi; KIS66950; KIS66950; UMAG_05731.
DR GeneID; 23565538; -.
DR KEGG; uma:UMAG_05731; -.
DR VEuPathDB; FungiDB:UMAG_05731; -.
DR eggNOG; ENOG502RDQF; Eukaryota.
DR OMA; FQAYLIP; -.
DR OrthoDB; 1493831at2759; -.
DR SABIO-RK; A0A0D1DWQ2; -.
DR PHI-base; PHI:8816; -.
DR Proteomes; UP000000561; Chromosome 16.
DR GO; GO:0048046; C:apoplast; TAS:PHI-base.
DR GO; GO:0044164; C:host cell cytosol; TAS:PHI-base.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:PHI-base.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0140502; P:effector-mediated suppression of host salicylic acid-mediated innate immune signalling; IDA:PHI-base.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR SUPFAM; SSF48600; SSF48600; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Glycoprotein; Host cytoplasm; Isomerase;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:30651637"
FT CHAIN 22..290
FT /note="Secreted chorismate mutase"
FT /evidence="ECO:0000255"
FT /id="PRO_5002240521"
FT REGION 117..140
FT /note="KWL1-binding extensive loop region (ELR)"
FT /evidence="ECO:0000269|PubMed:30651637"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 1..21
FT /note="Missing: Impairs secretion and ability to act as a
FT virulence factor."
FT /evidence="ECO:0000269|PubMed:30651637"
FT MUTAGEN 117..140
FT /note="Missing: Abolishes the interaction with host defense
FT KWL1."
FT /evidence="ECO:0000269|PubMed:30651637"
FT MUTAGEN 183
FT /note="R->A: Impairs catalytic activity; when associated
FT with A-193."
FT /evidence="ECO:0000269|PubMed:21976020"
FT MUTAGEN 194
FT /note="K->A: Impairs catalytic activity; when associated
FT with A-183."
FT /evidence="ECO:0000269|PubMed:21976020"
FT HELIX 29..47
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6FPG"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6FPG"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6FPG"
SQ SEQUENCE 290 AA; 31859 MW; CD8656BAFC0CE500 CRC64;
MKLSVSIFVL LAVSAFGGGS AAAVSGKSEA AEIEAGDRLD ALRDQLQRYE TPIIQTILAR
SALGGRAPSE QDEVRAALSR NAFEPSEVIS EWLQTESGAR FRSTRPLPPA VEFITPVVLS
RDTVLDKPVV GKGIFPIGRR PQDPTNMDEF LDTSLLSLNQ SSTVDLASAV SLDVSLLHLV
SARVLLGYPI ALAKFDWLHD NFCHILTNTT LSKSQKLANI IQQLTDHKQE VNVLSRVEQK
SKSLSHLFRN DIPYPPHTQD RILRLFQAYL IPITTQIEAA AILDHANKCT
