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Database: UniProt
Entry: A0A084Q9W9_STAC4
LinkDB: A0A084Q9W9_STAC4
Original site: A0A084Q9W9_STAC4 
ID   A0A084Q9W9_STAC4        Unreviewed;       448 AA.
AC   A0A084Q9W9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 35.
DE   RecName: Full=Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein {ECO:0000259|SMART:SM00922};
GN   ORFNames=S40285_04738 {ECO:0000313|EMBL:KFA60754.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60754.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA60754.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60754.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; KL660891; KFA60754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084Q9W9; -.
DR   STRING; 1283841.A0A084Q9W9; -.
DR   HOGENOM; CLU_030273_1_1_1; -.
DR   InParanoid; A0A084Q9W9; -.
DR   OMA; WGYAELR; -.
DR   OrthoDB; 33243at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0050032; F:L-rhamnonate dehydratase activity; IEA:InterPro.
DR   CDD; cd03327; MR_like_2; 1.
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; IPR023444; L-Rhamnon_dehydrat.
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   SFLD; SFLDF00006; rhamnonate_dehydratase; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT   DOMAIN          167..265
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   REGION          404..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  49426 MW;  C500CA9136D1272F CRC64;
     MRSFPTIKAI RSFVIGGVGS GGDYHNVKGG HWLIDSDIST PCSGWEQYRK SRTSWGINVL
     GSFLVEIEAT DGTVGFATGF GGPPACWLVH KHFERFLVGA DPRNTNLLFE QMYRASMFYG
     RKGLPLAVIS VIDLALWDLL GKIRDEPVYR LIGGATKERL NFYCTGPQPA AAKAAGFWGG
     KVALPFGPDE GHVGLRKNVE YLRKQREAVG PDFPLMVDCY MSLNVSYTIE IVKACLDLNI
     NWWEECLSPD DTDGFEQIKR AHPTIKFTTG EHEYSRYGFR KLIEGRNLDI IQPDVMWLGG
     LTELLRVSAH AAAYDIPVVP HASGPYSYHF VISQPNTPFQ EYLANSPDGS SVLPVFGDLF
     IDEPIPTKGF LTTADLDKPG FGLTLNPAAR SKLIPSNYLL EFPTQSLMPP SPPVDSLEKK
     DEEPKVNGGV VESLTSKVQE LTTSESTA
//
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