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Database: UniProt
Entry: A0A0N0MFR9_9PROT
LinkDB: A0A0N0MFR9_9PROT
Original site: A0A0N0MFR9_9PROT 
ID   A0A0N0MFR9_9PROT        Unreviewed;       320 AA.
AC   A0A0N0MFR9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KPH87903.1};
GN   ORFNames=GLUCOINTEAF2_0201985 {ECO:0000313|EMBL:KPH87903.1};
OS   Komagataeibacter intermedius AF2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH87903.1, ECO:0000313|Proteomes:UP000031553};
RN   [1] {ECO:0000313|EMBL:KPH87903.1, ECO:0000313|Proteomes:UP000031553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF2 {ECO:0000313|EMBL:KPH87903.1,
RC   ECO:0000313|Proteomes:UP000031553};
RA   Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J., Gonzalez-Garcia L.N.,
RA   Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT   "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2, Isolated
RT   from Kombucha Tea.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:KPH87903.1}.
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DR   EMBL; JUFX02000090; KPH87903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0MFR9; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000031553; 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; IPR029752; D-isomer_DH_CS1.
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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          54..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          117..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  34047 MW;  169F0F4D3C0983C0 CRC64;
     MTDHSSRLNE MPTVILTFPL PDLVTQRLGT QYHVESLLTP AARQAYVTHS GNLVRAIVTN
     GSTRLDGAFM DTMPNLCIIH TFGVGYEGVD VDAARARGIE VAYSPGTNAD SVADQAFALL
     LAVMRDIVPN DGLVRQGAWR PVRPVPPQLS GQKIGILGMG HIGQRIAARA AGFSMPVFYY
     SRRPRNQAQW TYCSSVMDMA ARVNVLAIAL PGGPETCHLV DADVLQALGP QGYVVNVGRG
     SVISNTALSD ALEKGIIAGA GLDVTEGEPD VPATLREQPN IVFSPHVGAR SPQSLLTCLD
     QVMTNLHAAL AGRSVHTPVP
//
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