CM1_MAIZE
ID CM1_MAIZE Reviewed; 312 AA.
AC B4FNK8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Chorismate mutase 1, chloroplastic {ECO:0000305};
DE Short=ZmCM1 {ECO:0000303|PubMed:21976020};
DE EC=5.4.99.5 {ECO:0000255|PROSITE-ProRule:PRU00516};
DE Flags: Precursor;
GN Name=CM1 {ECO:0000303|PubMed:21976020};
GN ORFNames=ZEAMMB73_Zm00001d043356 {ECO:0000312|EMBL:ONM37680.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP HOMODIMERIZATION, INTERACTION WITH USTILAGO MAYDIS CMU1, AND SUBCELLULAR
RP LOCATION.
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 [4] {ECO:0007744|PDB:6HJW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WTH L-TYROSINE.
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: May play a role in chloroplast biogenesis. {ECO:0000305}.
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:0000255|PROSITE-ProRule:PRU00516};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by tyrosine and
CC phenylalanine. Activated by tryptophan. {ECO:0000250|UniProtKB:Q9C544}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P42738}.
CC -!- SUBUNIT: Homodimer (PubMed:21976020). Interacts with Cmu1 of the fungal
CC pathogen Ustilago maydis (PubMed:21976020).
CC {ECO:0000269|PubMed:21976020}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21976020}.
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DR EMBL; CM007649; ONM37680.1; -; Genomic_DNA.
DR EMBL; CM007649; ONM37683.1; -; Genomic_DNA.
DR EMBL; BT038696; ACF83701.1; -; mRNA.
DR RefSeq; NP_001140378.1; NM_001146906.1.
DR PDB; 6HJW; X-ray; 2.50 A; A/B=1-312.
DR PDBsum; 6HJW; -.
DR AlphaFoldDB; B4FNK8; -.
DR SMR; B4FNK8; -.
DR STRING; 4577.GRMZM2G028369_P01; -.
DR PaxDb; B4FNK8; -.
DR PRIDE; B4FNK8; -.
DR EnsemblPlants; Zm00001eb152250_T001; Zm00001eb152250_P001; Zm00001eb152250.
DR GeneID; 100272431; -.
DR Gramene; Zm00001eb152250_T001; Zm00001eb152250_P001; Zm00001eb152250.
DR KEGG; zma:100272431; -.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_1_1_1; -.
DR OMA; LCDTMCL; -.
DR OrthoDB; 1087630at2759; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000007305; Chromosome 3.
DR ExpressionAtlas; B4FNK8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004106; F:chorismate mutase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR PANTHER; PTHR21145; PTHR21145; 1.
DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01802; CM_pl-yst; 1.
DR PROSITE; PS51169; CHORISMATE_MUT_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Isomerase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..312
FT /note="Chorismate mutase 1, chloroplastic"
FT /id="PRO_0000446624"
FT DOMAIN 58..312
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT REGION 16..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 58
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6HJW"
FT BINDING 190..193
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 190..193
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6HJW"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6HJW"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:6HJW"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:6HJW"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:6HJW"
SQ SEQUENCE 312 AA; 34920 MW; 5F143DCDCB46D3A3 CRC64;
MAFKLATKAA AASPAAAHRG GLARGPEGTS RVAFGPAPRN KGLRAANNSA TPVAKEERVD
RSEILTLDSI RQVLIRLEDS IIFGLLERAQ FCYNADTYDS NAFHMDGFGG SLVEYMVRET
EKLHAQVGRY KSPDEHPFFP EDLPEPRLPP MQYPRVLHPI ADSININKEI WKMYFDELLP
RLVKKGSDGN AGSSALCDTT CLQALSKRIH YGKFVAEAKF QESPEAYMPA IIAQDRDQLM
HLLTYETVER AIEHRVEAKA KIFGQEVNIG VEDNGSPPVY KIVPSLVAEL YSYRIMPLTK
EVQIAYLLRR LD
