ID B8LWC9_TALSN Unreviewed; 334 AA.
AC B8LWC9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:EED24240.1};
GN ORFNames=TSTA_076110 {ECO:0000313|EMBL:EED24240.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED24240.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; EQ962652; EED24240.1; -; Genomic_DNA.
DR RefSeq; XP_002341627.1; XM_002341586.1.
DR AlphaFoldDB; B8LWC9; -.
DR STRING; 441959.B8LWC9; -.
DR GeneID; 8102312; -.
DR VEuPathDB; FungiDB:TSTA_076110; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; B8LWC9; -.
DR OMA; IAWAYSD; -.
DR OrthoDB; 1111153at2759; -.
DR PhylomeDB; B8LWC9; -.
DR Proteomes; UP000001745; 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 CDD; cd12168; Mand_dh_like; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 15..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 123..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 36378 MW; 19B04AE5055E5A50 CRC64;
MSRPKVLLLG DIQHARKSWE ALNDIADLIT TKATNRTEFI QECKDGKLDG VVAAYRTFGS
VAITGLIDEE LVSVLPKSLL FLAHCGAGYD QIDVHACSER KSPIRVSNVP TAVDDATADV
NIFLIIGAIR NFNTGMQALR QGKWRGDPAP PLGHDPEGKV LGILGMGGIG RNLKKKAEAF
GMKVIYHNRR QLSENMAVGA EYVTFDELLA KSDVISLNLP LNKNTYHIIG KPEFDKMKDG
VVVVNTARGA VIDEAALVEA LDSGKVFSAG LDVFEEEPKI HPGLLGNPNV MLVPHMGTWS
YETHTAMEEW AISNVRQALE KGTLKSIVPE QADL
//
