ID A0A164ZSR2_9AGAM Unreviewed; 496 AA.
AC A0A164ZSR2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=L-mandelate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SISNIDRAFT_404967 {ECO:0000313|EMBL:KZS98024.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS98024.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS98024.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS98024.1,
RC ECO:0000313|Proteomes:UP000076722};
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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; KV419396; KZS98024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164ZSR2; -.
DR STRING; 1314777.A0A164ZSR2; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000076722; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02922; FCB2_FMN; 1.
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; IPR037458; L-MDH/L-LDH_FMN-bd.
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; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722}.
FT DOMAIN 14..103
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 131..488
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 496 AA; 54150 MW; 1DD917AF8F76D286 CRC64;
MPDFSQINPS AKKTGLVSFD EVKAHAGRDS CWVVIGDKVW DVTSLLPNHP GGTNAILEQA
GTDVTLAPGL PTNSFVHRRL FDRLHSHDVL DLLPPGSLVG YVDQDTLPKI VHDDPLTEEE
LRILKARESL PPPSAALNLK DIERFAQQVL TETAWAYYSS AGDDEYTLHE NSAAFKRYWF
RPRVLNKVSR VSTSTTLFGS ETSLPIFIAP AALARLGHPG GEVNMVRVAG EEGIVQGISN
NASCSLDEIV SARRPGQPLV FQLYMNRERA ASEALVRRVE REGFNAIVLT VDAAVPGKRE
RDQRAKGNYS GIVPNGSSPP AGKGVAHAIS GYQDPDVDWA DVKWLQSITS LPLILKGIQC
VEDAELAFEN GVQGIVLSNH GGRELDFAPA PLTVLHELQH KRPDLVRERD VYIDGGVTRG
TDVLKALCLG AKGVGLGRAF LYGNGVWGED GVRRVIEIMR GEIETGMQLM GVTSIKDLKP
ELIRYVDRDL PPIASR
//
