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CM2_MAIZE
ID   CM2_MAIZE               Reviewed;         253 AA.
AC   B4FUP5; B4FAF1;
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 2, cytosolic {ECO:0000305};
DE            Short=ZmCM2 {ECO:0000303|PubMed:21976020};
DE            EC=5.4.99.5 {ECO:0000255|PROSITE-ProRule:PRU00516, ECO:0000269|PubMed:21976020};
GN   Name=CM2 {ECO:0000303|PubMed:21976020};
GN   ORFNames=ZEAMMB73_Zm00001d015509 {ECO:0000312|EMBL:AQK69073.1};
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].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [3]
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   [4]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, HOMODIMERIZATION, INTERACTION WITH
RP   USTILAGO MAYDIS CMU1, AND SUBCELLULAR 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   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
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   -!- 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         ECO:0000269|PubMed:21976020};
CC   -!- ACTIVITY REGULATION: No allosteric regulation.
CC       {ECO:0000269|PubMed:21976020}.
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: Cytoplasm, cytosol {ECO:0000269|PubMed:21976020}.
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DR   EMBL; CM000781; AQK69073.1; -; Genomic_DNA.
DR   EMBL; EU951879; ACG23997.1; -; mRNA.
DR   EMBL; BT034089; ACF79094.1; -; mRNA.
DR   EMBL; BT040833; ACF85838.1; -; mRNA.
DR   RefSeq; NP_001130752.1; NM_001137280.1.
DR   PDB; 6H3P; X-ray; 2.70 A; A/B=1-253.
DR   PDBsum; 6H3P; -.
DR   AlphaFoldDB; B4FUP5; -.
DR   SMR; B4FUP5; -.
DR   STRING; 4577.GRMZM2G179454_P01; -.
DR   PaxDb; B4FUP5; -.
DR   PRIDE; B4FUP5; -.
DR   EnsemblPlants; Zm00001eb234080_T001; Zm00001eb234080_P001; Zm00001eb234080.
DR   GeneID; 100191856; -.
DR   Gramene; Zm00001eb234080_T001; Zm00001eb234080_P001; Zm00001eb234080.
DR   KEGG; zma:100191856; -.
DR   eggNOG; KOG0795; Eukaryota.
DR   HOGENOM; CLU_057757_0_0_1; -.
DR   OMA; VGRYDNP; -.
DR   OrthoDB; 1087630at2759; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; B4FUP5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..253
FT                   /note="Chorismate mutase 2, cytosolic"
FT                   /id="PRO_0000446625"
FT   DOMAIN          2..253
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT   CONFLICT        130
FT                   /note="G -> A (in Ref. 3; ACF79094)"
FT                   /evidence="ECO:0000305"
FT   HELIX           11..32
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           53..67
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           108..117
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           132..151
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           153..163
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           177..184
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           187..205
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           225..234
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   HELIX           236..248
FT                   /evidence="ECO:0007829|PDB:6H3P"
FT   TURN            249..252
FT                   /evidence="ECO:0007829|PDB:6H3P"
SQ   SEQUENCE   253 AA;  28326 MW;  BC7AE58682F928E9 CRC64;
     MDAAGGDQLS LAAVRDALVR LEDSVVFALI ERARHPRNAP AYAPAATAGE HSLVEFFVRE
     AEALNAKAGH YQKPEDVPFF PQDLPSPLFP TKPSPKVLHP FASLVTVNDA IWKMYFDELL
     PLFTVDGDDG SYAQTVALDL ACLQVLSQRI HIGKYVAEVK FKDAPQEYSR LIKEKDSNSL
     MDMLTFKAVE EKVKKRVEKK ARTFGQNVTL DDNATAGDSE CKVDPKVLSK LYDQWVMPLT
     KDVEVEYLLR RLD
 
 
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