ID G8YGV0_PICSO Unreviewed; 533 AA.
AC G8YGV0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Piso0_002979 protein {ECO:0000313|EMBL:CCE80652.1};
GN Name=Piso0_002979 {ECO:0000313|EMBL:CCE80652.1};
GN ORFNames=GNLVRS01_PISO0G02228g {ECO:0000313|EMBL:CCE79887.1},
GN GNLVRS01_PISO0H02229g {ECO:0000313|EMBL:CCE80652.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE80652.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE80652.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; FO082053; CCE79887.1; -; Genomic_DNA.
DR EMBL; FO082052; CCE80652.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YGV0; -.
DR STRING; 559304.G8YGV0; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; G8YGV0; -.
DR Proteomes; UP000005222; Chromosome G.
DR Proteomes; UP000005222; Chromosome H.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222}.
FT DOMAIN 99..278
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 533 AA; 59006 MW; 7C97BDC6A9CB19DA CRC64;
MISIKQAIPR GLSVARTLAP RSFRLVYRQS NITPVSFYSS KVIPLTAESY ADKVKRDERY
SKLNDSDIEA FKSILQDSHS LITNEDDVAF FNEDWMRKYR GQTKLVLKPK TTEQVSEILR
YCNERNLAVV PQGGNTGLVG GSIPIFDEII ISLGSLNKIR SFDSVSGVLK CDAGLILQNA
DEFLKEQGYI FPLDLGAKGS CHVGGNVATN AGGLRLLRYG SLHGSVLGLE AVLPDGTIYS
SMDALRKDNT GYDLKQLFIG SEGTLGIITG VSILCPSRPQ AFNVALLAVS SYEAVQKVFV
GARRELSEIL SAFEFMDGKS QLLTSRHLKA DHPIESGEYP FYILIETSGS NKDHDDEKLE
AFLEKAMEDG LVDDGIIAQD ETQVQNLWAW RESIPEASTI GGGVYKYDVS LPLADLYGLV
EAASERLSQE GLVDIDDASK PVVEAIGYGH VGDGNLHLNV AVREYSKRVE NVLEPFIYEW
IQSKKGSISA EHGLGFQKKN YIGYSKTDIE IKLMKDLKEH YDPKLIMNPY KYI
//
