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Database: UniProt
Entry: E1QZL6_OLSUV
LinkDB: E1QZL6_OLSUV
Original site: E1QZL6_OLSUV 
ID   E1QZL6_OLSUV            Unreviewed;       407 AA.
AC   E1QZL6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ADK67830.1};
GN   OrderedLocusNames=Olsu_0716 {ECO:0000313|EMBL:ADK67830.1};
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67830.1, ECO:0000313|Proteomes:UP000000333};
RN   [1] {ECO:0000313|EMBL:ADK67830.1, ECO:0000313|Proteomes:UP000000333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC   VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(2010).
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; CP002106; ADK67830.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1QZL6; -.
DR   STRING; 633147.Olsu_0716; -.
DR   KEGG; ols:Olsu_0716; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_9_0_11; -.
DR   Proteomes; UP000000333; Chromosome.
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   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd12174; PGDH_like_3; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF55021; ACT-like; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000333}.
FT   DOMAIN          38..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          131..284
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   407 AA;  44109 MW;  72FF54631FBAF786 CRC64;
     MRSQRGIPVR HVKIMDNISR KITRDGIVDL GEGYERYEDV NGADAILVRA SDIHGMDLGP
     NVRCVARSGA GYNNIPIEDC ARRGIVVFNT PGGNSNAVKE LVVGMILVNS RGTLGGINWV
     LDNAQDPDIV RDAERNKKAF VGHEAIGRKV GVVGLGAVGS KVANALVSLG LDVHGYDPYL
     SVEHAWQLSR SVKRVDSLDE LCRDADYVSL HVPSKDDTVR MIGARQIALM HEGAMLVNYA
     RADIIDEDAV AAALKDGRLG SLVCDFATPK TTRMPRTMIT PHMGACTNEA EENCAAMAVS
     QMKDYLESGI IRNSVNYPDC DLGPVTSGLR IAALHDNVPN MIGQITAVLA RYDANIRRMS
     NEAQDGSAYT LIDLDGRLDD GAVADLRPIP GIYRIRVLEP PREATRA
//
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