ID A0A0J0XQJ2_9TREE Unreviewed; 529 AA.
AC A0A0J0XQJ2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=L-mandelate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC85DRAFT_284510 {ECO:0000313|EMBL:KLT43363.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT43363.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT43363.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT43363.1,
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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; KQ087195; KLT43363.1; -; Genomic_DNA.
DR RefSeq; XP_018279854.1; XM_018422776.1.
DR AlphaFoldDB; A0A0J0XQJ2; -.
DR STRING; 879819.A0A0J0XQJ2; -.
DR GeneID; 28983379; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR PANTHER; PTHR10578:SF101; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT DOMAIN 69..146
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 172..529
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 529 AA; 57392 MW; 9DD6ED0D56335258 CRC64;
MFARPLARAA RAGRTSARRF ASSSTSVAGS RLATRLTLAA AGAAVIAGTT YAFLPQAHAD
ASRITKAGER IITLEELGKH WQAGSLWVAV DGKVYDVSEF ANVHPGGLRI LLENGGRDAT
KLFHAIHPPN TIKKYTKQVP CVGVIDPEEL AVLASQRSAE DDRIETARRS LFGVDSVVGL
SDFERYAKDL LPLHAWAYYS TGADTEGALA ENTAIFRRIF FRPRIMRDVH DVDTSTEFLG
VKSSIPVYVA PTARNGLGQP EGEVAVTRGA GATGIFQVLS HYASRSLDEV KAAAREGQQI
GWQLYLNPDR ERSREAIEDA VAAGAHSIWI TADTVTLGKR ETERRLNAEA NPAPNGKPLS
RERQRFGFSA HDTRMSWDDI AFVRKHAPGL PVIVKGVGAW EDVVLAYKYG ADAVVLSNHG
GRQLDFAQPP MKVLYDVNKN APQVLHRKNF NIFLDGGVRT GTDVLKALCL GATAVGLGRP
FIYAATGWGS DGVEKAVQLL EEEITIGMQL LGVTRVDQLG PQYLDTSKI
//
