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Database: UniProt
Entry: I4MW71_9PSED
LinkDB: I4MW71_9PSED
Original site: I4MW71_9PSED 
ID   I4MW71_9PSED            Unreviewed;       304 AA.
AC   I4MW71;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=NAD-binding D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:EIK93461.1};
GN   ORFNames=PMM47T1_26752 {ECO:0000313|EMBL:EIK93461.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK93461.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK93461.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK93461.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(2012).
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:EIK93461.1}.
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DR   EMBL; AJWX01000037; EIK93461.1; -; Genomic_DNA.
DR   RefSeq; WP_008374984.1; NZ_AJWX01000037.1.
DR   AlphaFoldDB; I4MW71; -.
DR   STRING; 1179778.PMM47T1_26752; -.
DR   PATRIC; fig|1179778.3.peg.5310; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000004339; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339}.
FT   DOMAIN          34..300
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          97..269
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   304 AA;  31961 MW;  AD24FEBBFCA2BECE CRC64;
     MPHDLLVLID LSPARSQRLE AAGYRLHVTP SAAIEAVLTN GSIGFTAQQM TDVPRLGIIC
     AQGAGYENID LAAARARGIV VTHGPGTNDE SVADHALALL LAVVRDIPQA DRAVREGRWA
     QSRHPRPMLS NKKLGILGLG TIGQKVARRG ELGFGMAVGY HNRQPRQGTC ATYFDTLPGL
     AAWADFLLVA TPGGVGTRHL INDAVLAALG SEGYLVNIAR GSVVDNAALT RALAQGTIAG
     AALDVVDGEP LIPTPWLALD NLILTPHIAG RSPEAMQATL QQVLDNLDAF FVGQPVPTPV
     PELS
//
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