ID A0A194Q2P9_PAPXU Unreviewed; 328 AA.
AC A0A194Q2P9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0000313|EMBL:KPI99821.1};
GN ORFNames=RR46_04795 {ECO:0000313|EMBL:KPI99821.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI99821.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI99821.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI99821.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI99821.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; KQ459562; KPI99821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194Q2P9; -.
DR STRING; 66420.A0A194Q2P9; -.
DR Proteomes; UP000053268; 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; cd05301; GDH; 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; 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:SF119; FI03731P-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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:KPI99821.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268}.
FT DOMAIN 14..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 118..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35654 MW; 33A2423CEE62E9C8 CRC64;
MTKLKVLVSS NDYLDSGIKI LEEHFTVVKS RYQNFSEEGL TKNKDELLDL IPGCSALVWV
SHHPITKELL DRAGPQLKVV STASAGYNHC NVPELKKRGI KLANTPGVLS AAVAEVAIAL
MLGAARRFTE NLDQVHSGEW EIGFDKVLGQ DIQGSTVGIV GLGGIGQATV KRLRGFDVEK
FLYTGHREKP EAKELGAEFV DLDTLLAHSD FVVLAVPLTD ETKHMINKTT LAKMKKNAIL
VNVGRGDLVN QDDLYDALKN RDIYSAGLDV TTPEPLPKDH KLLTLPNIFI LPHIGSATIG
TRNAMSVLAA KNVVNALNGK PLITPVLE
//