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Database: UniProt
Entry: E6ZZH7_SPORE
LinkDB: E6ZZH7_SPORE
Original site: E6ZZH7_SPORE 
ID   E6ZZH7_SPORE            Unreviewed;       501 AA.
AC   E6ZZH7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   28-JUN-2023, entry version 43.
DE   RecName: Full=Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein {ECO:0000259|SMART:SM00922};
GN   ORFNames=sr13336 {ECO:0000313|EMBL:CBQ72657.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72657.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ72657.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FQ311470; CBQ72657.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZZH7; -.
DR   EnsemblFungi; CBQ72657; CBQ72657; sr13336.
DR   VEuPathDB; FungiDB:sr13336; -.
DR   eggNOG; ENOG502QU7C; Eukaryota.
DR   HOGENOM; CLU_030273_2_0_1; -.
DR   OrthoDB; 2903547at2759; -.
DR   Proteomes; UP000008867; Chromosome 5.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
FT   DOMAIN          228..348
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   REGION          271..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  55130 MW;  32DDF4C28AC897ED CRC64;
     MTRSSPLIVS SYSIHDVRFP TSLTGDGTDA MNKTCDYSAA YLILYTSLKD DAEIVSYRGR
     ESESINAPVK EDNSLRGFGM TFTIGKGNEI CCQAIASIVE ELLLGREIEP LFANMGETWQ
     LMVSDPQLRW IGPEKGVIHL ATAAVINAIW DLYARSRSKP LWKLICDMSP EELVQCVPFR
     YITDAITPAE ALKILQDSAK GKAQREAEMV ANGYKAYTTS AGWSGYDDAK VARLTRSALE
     QGFNHFKLKV GADVADDIRR LSLMRSIIDD PKEMPAGREQ PSPESLAGKN AGPTGCVVMV
     DANQVWDVQE AIDYMEKLAH LRPWFIEEPT APDDVLGHAA IRRGIKHLGI GVATGEHAHN
     RMTFKQLLQA DAIDVVQIDS CRLAGVNEIL AVMLMAKKFG KIVCPHAGGV GLCEYVVHLS
     LIDYICISAT NERNVLEWVD HLHEHFVYPV SINGAGCYNT PVDPQGGYSI EMLKSSIEDY
     SFPQGSYWKS GTARTAPPSG H
//
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