ID C0QQQ9_PERMH Unreviewed; 321 AA.
AC C0QQQ9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glycerate dehydrogenase (NADH-dependent hydroxypyruvatereductase) (Hpr) (Gdh) (Hydroxypyruvate dehydrogenase) (Glyoxylatereductase) (Hpr-a) {ECO:0000313|EMBL:ACO03240.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:ACO03240.1};
GN OrderedLocusNames=PERMA_1233 {ECO:0000313|EMBL:ACO03240.1};
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Persephonella.
OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03240.1, ECO:0000313|Proteomes:UP000001366};
RN [1] {ECO:0000313|EMBL:ACO03240.1, ECO:0000313|Proteomes:UP000001366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001230; ACO03240.1; -; Genomic_DNA.
DR RefSeq; WP_012675479.1; NC_012440.1.
DR AlphaFoldDB; C0QQQ9; -.
DR STRING; 123214.PERMA_1233; -.
DR PaxDb; 123214-PERMA_1233; -.
DR KEGG; pmx:PERMA_1233; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_0; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001366; Chromosome.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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:ACO03240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001366}.
FT DOMAIN 15..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 36119 MW; 5C0A20EAE5D9294C CRC64;
MKIVFLDAKT VGDDIDLSVF EAFGDFIAYP TTKGSEVFDR VYDADIIITN KVIIDREVID
YARDLKLICV AATGTNNVDI LYAKEKGIAV TNVAGYSTES VVQHTFAMLF YILEQLRYYD
DYVKSGQYAE SDIFTHLGRP FSEINGKRWG IIGLGTIGRR VGQVAESFGC DVIYHSTSGV
KREERYREYP LDELLKTSDI VSIHAPLNEK TRNLITYDKI SLMKPSAILL NLGRGGIVNE
EDLARALDEG LISGAGLDVL EKEPIDPYSP LLSIKNRDRL LITPHIAWTS IEARKRLIQE
IAENIRAFLN GKERNRVDLV F
//
