ID A9UR17_MONBE Unreviewed; 287 AA.
AC A9UR17;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MONBRDRAFT_19417 {ECO:0000313|EMBL:EDQ92697.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ92697.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ92697.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CH991543; EDQ92697.1; -; Genomic_DNA.
DR RefSeq; XP_001742459.1; XM_001742407.1.
DR AlphaFoldDB; A9UR17; -.
DR STRING; 81824.A9UR17; -.
DR EnsemblProtists; EDQ92697; EDQ92697; MONBRDRAFT_19417.
DR GeneID; 5887919; -.
DR KEGG; mbr:MONBRDRAFT_19417; -.
DR eggNOG; KOG0069; Eukaryota.
DR InParanoid; A9UR17; -.
DR OMA; IAWAYSD; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357}.
FT DOMAIN 2..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 77..255
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 287 AA; 30431 MW; 95B116F32E19DB0F CRC64;
MPRAELLEAV KGAHGIVCML SDKIDKEVIE AAGPNLKCIS TLSVGFNHID VDECKTRGIK
IGNTPGVLTN ATADLALSLL LATCRLIPQA VHEAKNGGWG TWKPMWLCGT ELAGKTVGIV
GMGRIGSAVA KRLRAFEIGR LLYSGRSEKP NAKELQAEFV DVDTLLREAD IVVATCALAP
ETTNIFNADA FKKMKNTAIL VNAARGACVD QDALVEALKA GEIKAAGLDV TTPEPLPTDH
ELFKLPNCVI LPHIGSATDE CRSIMAVMTA ENCVKGISGE DMPAQVC
//
