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Database: UniProt
Entry: A0A095B7T7_9SPHN
LinkDB: A0A095B7T7_9SPHN
Original site: A0A095B7T7_9SPHN 
ID   A0A095B7T7_9SPHN        Unreviewed;       314 AA.
AC   A0A095B7T7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:KGB57759.1};
GN   ORFNames=FG95_01604 {ECO:0000313|EMBL:KGB57759.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB57759.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB57759.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB57759.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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:KGB57759.1}.
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DR   EMBL; JNFC01000017; KGB57759.1; -; Genomic_DNA.
DR   RefSeq; WP_037555160.1; NZ_JNFC01000017.1.
DR   AlphaFoldDB; A0A095B7T7; -.
DR   STRING; 1120705.FG95_01604; -.
DR   PATRIC; fig|1120705.3.peg.1629; -.
DR   eggNOG; COG0111; Bacteria.
DR   OrthoDB; 9787219at2; -.
DR   Proteomes; UP000029625; 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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT   DOMAIN          29..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          107..276
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   314 AA;  34398 MW;  9B6F44361423DD4D CRC64;
     MSKTVTVLSG LIRPLVENRL PDWVEPRFFQ SKEEALELAP HAEIGWFDMY DKKDMAAVIT
     AATNLKWLNS IYAGVDGMPL DLLAERGTVV TNGAGINAIT IAEYVVMGML TVAKGYRDVV
     RAQERREWLI DSPGKVELFG SRALLLGYGA IGKLIEERLK AFAVDVTVVR RSPGPNTLTP
     DQWRARLGDF DWVILAVPAT PETDGMIGAA ELAAMKPTAT LINIARGSVV DQGALVAALD
     SQQIASAFLD VTTPEPLPAD DPLWSLDNAH ITMHLSGRAQ DKMFVRSAQR FLENLGRWKK
     GEAVEPRVDL TLGY
//
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