ID A0A0J1B3W2_9TREE Unreviewed; 427 AA.
AC A0A0J1B3W2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Putative racemase {ECO:0000313|EMBL:KLT42334.1};
GN ORFNames=CC85DRAFT_274445 {ECO:0000313|EMBL:KLT42334.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT42334.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT42334.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT42334.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ087206; KLT42334.1; -; Genomic_DNA.
DR RefSeq; XP_018278825.1; XM_018421368.1.
DR AlphaFoldDB; A0A0J1B3W2; -.
DR STRING; 879819.A0A0J1B3W2; -.
DR GeneID; 28981971; -.
DR OrthoDB; 33243at2759; -.
DR Proteomes; UP000053611; 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; SFLDG00179; mandelate_racemase; 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:UP000053611}.
FT DOMAIN 169..267
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT REGION 404..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 47033 MW; 1CC4A2C0CE6D9810 CRC64;
MPEWPTIAKL ETFIPSATGS GGDYHRQANE HWIVQGNISC PMHKYDEYRS SRTSWGIGVL
GSIFVKITAS DGTVGYATGF GGPPACWLIE EHYKRFIVGQ DPRDTNKMWD MMFRASMFYG
RKGLPLAAIS VVDLAIWDLI GKIRGEPIYK MIGGRTKKDI PLYLTGPKPA VAKKLGFWGA
KVPLPHGPPD GPAGIRANVA YLKAAKESVG PDFPVMVDCY MSLDVPYTIE LVRACEAAGL
HMHWWEECLH PDDFDGHAEL HRALPHVKFT TGEHEYSKYG FRKLIEGRNL AIIQPDVMWL
GGLTELIKVA NMAAAYDIPV VPHGSGPYSF QAIMSFPNSD FCEYIANSPD GESIHPSFGD
LFTNEVLPTN GRIDLSDAPG WGLELNPNAK LVPYSTFFAP AGGLGSAGED RTEEEQEKFK
GKVTNGH
//
