ID A0A150V5Z0_9PEZI Unreviewed; 364 AA.
AC A0A150V5Z0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN ORFNames=M433DRAFT_66173 {ECO:0000313|EMBL:KYG45947.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45947.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG45947.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG45947.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG45947.1}.
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DR EMBL; JPDO01000137; KYG45947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V5Z0; -.
DR STRING; 766039.A0A150V5Z0; -.
DR Proteomes; UP000075602; 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:UP000075602}.
FT DOMAIN 122..198
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 233..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 364 AA; 40370 MW; C0431ADDEB735255 CRC64;
MGGGPDHLLI LLPQPEPAEI INGLRKKFPN IKITYREVTF HGPGTNDLTD PLPDEIWKDV
TILYTLFTLP EKISYASKLQ LIQLASAGSN QVQNHPIYTK TDIIITTSSG IHGPQIAEWA
VMTALVQSHH YNKLHDLQKE HKWGSKDMSE YRNVKDNVGR TLGVLGYGSI GRQVGRVAQA
MGMNVVAYTA TPKDTPEKRK DNGFVLPGTG DPDGSIPSAW YSGLDVESRR KFLAQDIDWL
LVSVPLTNET RHFLSMPEFK ILGREGNKPA FITNIARGPI IDQPKLIAAL KDGLLSGAAL
DVSDPEPLPA DNELWDLPNV IITPHISGSS QAYSERSFQV LEENLKRREN GLKLLNVVRR
SRGY
//
