ID A0A1V6RYZ4_9EURO Unreviewed; 360 AA.
AC A0A1V6RYZ4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN ORFNames=PENVUL_c015G09442 {ECO:0000313|EMBL:OQE07011.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE07011.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE07011.1}.
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; MDYP01000015; OQE07011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RYZ4; -.
DR STRING; 29845.A0A1V6RYZ4; -.
DR OrthoDB; 1775226at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12163; 2-Hacid_dh_5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 2.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT DOMAIN 119..190
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 226..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 360 AA; 39412 MW; BDF12BC014F464A7 CRC64;
MGDAPLSSEH VLVVFYRAMP AELSDVIRHK FSNAEVTIYQ SQQGIPLPSE LYQRATVLVT
FTDLPELKDS KNLKLIHTFS AGVDHLLKHP ILRESDIPIT TSSGIHGPPI AEWTVMNWLV
SSRKYVHTYE SQKSHIWGDK NAYTQGLHDQ VGKKVGILGY GSIGRQIARV SHALGMTVHA
YTANPRPTPE SRHDQGYIVP GTGDPDGSIP ASWHHGTDRE SIRSFLATGL DHLVISLPLT
PETTRLLGAE EFAILSDNCH HHASKPYVTN ISRGKVIDQK ALGDALNSGV LGGAALDVTD
PEPLPKDDPL WDASNVQISP HVSGLGMEYF PRSLDILVLN LGRIARGEPL INAYVRGKGY
//