ID A0A182JR51_9DIPT Unreviewed; 372 AA.
AC A0A182JR51;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR000983-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR000983-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR000983-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR AlphaFoldDB; A0A182JR51; -.
DR STRING; 43041.A0A182JR51; -.
DR EnsemblMetazoa; ACHR000983-RA; ACHR000983-PA; ACHR000983.
DR VEuPathDB; VectorBase:ACHR000983; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000075881; 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; 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:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 66..371
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 162..341
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 372 AA; 41130 MW; 329322632486A1F3 CRC64;
MNPVFRQLSA ALSSGSSLRG SIRLGIVLRR QPVCAARAVT IQPQRRYCCL EMKPKVYVTR
NDYARIGLDL LREECDISLW DEAYPVPRDE FLKNVAGKDA IYCSLNDRID KELLDQAGPN
LKVISTISVG YDHIDVKECK QRGIRIGYTP DVLTDATAEL TVALLLATAR RMFEANKQVH
TGGWKSWSPM WMCGKSVKNS VVGIFGFGRI GQEVAKRLAP FKPSHIQFTS RTDKFLTAED
LGVTQVPFDE LIETSDFLII ACSYNVETAN LFNDAVFSRM KPSAILINTS RGGVVEQHDL
IHALRAGKIQ AAGLDVTTPE PLPLDNPLLT LPNVVVLPHI GSADIETRIE MSRITACNIL
AGLKGIKMMS EV
//
