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Database: UniProt
Entry: A0A102D6R6_9SPHN
LinkDB: A0A102D6R6_9SPHN
Original site: A0A102D6R6_9SPHN 
ID   A0A102D6R6_9SPHN        Unreviewed;       316 AA.
AC   A0A102D6R6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KUR75984.1};
GN   ORFNames=AQZ49_13160 {ECO:0000313|EMBL:KUR75984.1};
OS   Novosphingobium sp. FSW06-99.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR75984.1, ECO:0000313|Proteomes:UP000061032};
RN   [1] {ECO:0000313|EMBL:KUR75984.1, ECO:0000313|Proteomes:UP000061032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR75984.1,
RC   ECO:0000313|Proteomes:UP000061032};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUR75984.1}.
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DR   EMBL; LLZQ01000018; KUR75984.1; -; Genomic_DNA.
DR   RefSeq; WP_067616368.1; NZ_KQ954257.1.
DR   AlphaFoldDB; A0A102D6R6; -.
DR   STRING; 1739113.AQZ49_13160; -.
DR   Proteomes; UP000061032; 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; cd12156; HPPR; 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:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061032}.
FT   DOMAIN          53..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..280
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   316 AA;  33117 MW;  966C4FE616B0561E CRC64;
     MSDPARPDIL VAAPLPAFTM DVLEARFTVH KLWQGVAPAD LARVRGMAAS TLAGPVGEAL
     FAQIPGLEIV ANFGVGYDNI DMAAAVARHL VVTNTAGVLD EEVADLTVGL LLATVRRIPA
     AERYVRDGLW PGGGFALSPS LRGRRVGIVG LGGIGKAVAR RLAGFAVDIA WYGRSEQPDV
     AWPRYPSVEA LAAACDVLIV IVPGGAATRH LIDARVLAAL GPDGVLINVA RGSVVDEAAL
     IEALQARTIL AAGLDVFEHE PHVPQALLAC DNAVVLPHIG SASLVTRQAM GRMMADNLTA
     WFTTGRALTP VPETRY
//
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