ID A0A179GNV3_PURLI Unreviewed; 352 AA.
AC A0A179GNV3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:OAQ79452.1};
GN ORFNames=VFPFJ_09938 {ECO:0000313|EMBL:OAQ79452.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ79452.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ79452.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ79452.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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:OAQ79452.1}.
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DR EMBL; LSBI01000010; OAQ79452.1; -; Genomic_DNA.
DR RefSeq; XP_018174469.1; XM_018327007.1.
DR AlphaFoldDB; A0A179GNV3; -.
DR STRING; 33203.A0A179GNV3; -.
DR GeneID; 28892056; -.
DR KEGG; plj:VFPFJ_09938; -.
DR OMA; KHGAWQQ; -.
DR OrthoDB; 2900331at2759; -.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12169; PGDH_like_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT DOMAIN 43..348
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 124..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 352 AA; 38143 MW; FCC780C7EFBDC917 CRC64;
MALKIAVLDD YQGCAKQFYD KLDGSKYAVS YFPDTLLPYN VAPREVQDEL VQRLEPFDVI
SCMRERTPFP AALLQRLPNL KLLLTTGVRN KAIDLPSCAA RRIPVAGATD THAGPADSTT
EHAVAMILGV ARGLASNDAN VKAGLWQTGF ATGLAGGTLG VLGLGRLGAA VARAMHLALG
MKVIAWSTNL TQEAADEQAR HAGLPVEGPD GEKTFRAVSR EELFSMADVV SVHLVLSDRT
RGIVNAQDLG RMKPSAFFVN TSRGPLVVER DLLDVLKAGK IRGAALDVFD LEPLPRDSEW
RSAEWGKNGR SEVLIAPHMG YVEERSISGF YRKQVANLER WVAGEPLETL LA
//
