ID A0A1Y1YRD2_9FUNG Unreviewed; 784 AA.
AC A0A1Y1YRD2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=VOC domain-containing protein {ECO:0000259|PROSITE:PS51819};
GN ORFNames=K493DRAFT_312792 {ECO:0000313|EMBL:ORY00583.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY00583.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORY00583.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY00583.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY00583.1}.
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DR EMBL; MCFE01000081; ORY00583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YRD2; -.
DR STRING; 1314790.A0A1Y1YRD2; -.
DR InParanoid; A0A1Y1YRD2; -.
DR OrthoDB; 2581705at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037523; VOC.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193498}.
FT DOMAIN 619..758
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 784 AA; 87912 MW; 94DEEC3971EE12F7 CRC64;
MATPSIQSFS PSEFVTVKSI TYDNGLPFTI FEWKDCETNA IGWIAIDGSQ PRTAGGGLFM
SSSATLMEVC DIANTMSNKM CVSRISTVRG AKGGIRFDHT DPRAQEVLRR FFRDNKSVLL
NYWGTGADLN TDHHVIDVLF KEEIGISTAL YSIYKAHGLE NEINILHKPL TMDVNEFFNL
SEASVGYGAA VSLFELMKVR NPELIGKARV IIQGFGTVGS TFAYYLKELG IGRVVGIMSI
DGIYVDDNID VLELLRVRHA RRDEAGLDIK SVEACLTPEQ LASSAYSKRD ENENDQDYLL
RFIKSTQADV WAPCAGRYCL TAEIASALVE TTFASSDDRS RFILAGANNV FGKWEEGQSK
RTSPQEQAAL LGCLTDAGVQ MLPEWVTNSG TSCLFMLTCT RQYSDEESVT KVILEDIRND
ITEFIQRAAL VDQTLNSYEC CSKYAQAIRQ QRELEGRRKD LVISKIHHYH IVTQDLTVPL
KFYQENMACE IKMIDGSNAS YNDRRFTRQC VIRFLTKEDP FLIISEDPAS AITDCGIDYL
AFSASDIDLV TDTLKQNFVS FDLVKSHPLW TVGGLNIPAE DRGYGFVILE DAFDVTNFHD
ISMKPLPPLS TEPALAHTGI DHYTLIVDDA DKVKDFHVNI LGYKHINTIR LNVGTAPEGE
HDMLNHVMGV PNDHHRVLVI TSGLTEESVF RKLLQKKGHG FVHHIAHQVE DIEGAFEKMK
ASSYKLTMDQ IKHDMILGLK QIFIADDYVH HFVELVERTE RSNLQGTFVD DNITALAQSM
NRYV
//