ID   A0A165EYA8_9BASI        Unreviewed;       471 AA.
AC   A0A165EYA8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative mandelate racemase/muconate lactonizing enzyme {ECO:0000313|EMBL:KZT55775.1};
GN   ORFNames=CALCODRAFT_498247 {ECO:0000313|EMBL:KZT55775.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT55775.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT55775.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT55775.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; KV423989; KZT55775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165EYA8; -.
DR   STRING; 1353952.A0A165EYA8; -.
DR   InParanoid; A0A165EYA8; -.
DR   OrthoDB; 2903547at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
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; IPR013341; Mandelate_racemase_N_dom.
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   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   DOMAIN          199..318
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   471 AA;  51898 MW;  CE25F760EB91BAF7 CRC64;
     MSPTITAFEV KDIRFPTSLN GAGSDAMNVD VDYSAAYIAL HTSDPALSSY GMTFTIGRGT
     EIVCEAIEQV AARLIGKDVE GLFSNMGETW TFLVSDYQLR WVGPEKGIIH LATAAVDNAL
     WDMYARARKK PLWKLVADFT PEEFVKSTAF RYITDMITPE EALEMLKAKE AGKKEREELV
     REIGYPAYIT SAGWLLYDDE QVSRLTKEAI GRGFNHFKMK VGADLQDDLR RAKLIRSIID
     NPANLSPGKV IDPKSIEGKN AGPTGSVLMM DANQVWDVQE AIDYVIQLAP TKPWFIEEPT
     APDDILGHAA IRKALKPYGI GVATGEHAHN RMIFKQLLEA NAIDVCQIDS CRLAGVTEIL
     GVLLMAAKSG VIVCPHAGGV GLCEHALHLS LIDYICVSGT MERNVLEYAD HLHEHFVAPV
     TLNTNGRYNV PNDPEQGYST HMKDSAFEEF GFPDGAYWKS VAEGKPKAVL M
//