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Database: UniProt
Entry: A0A023D8Q1_ACIMT
LinkDB: A0A023D8Q1_ACIMT
Original site: A0A023D8Q1_ACIMT 
ID   A0A023D8Q1_ACIMT        Unreviewed;       309 AA.
AC   A0A023D8Q1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:GAJ30494.1};
GN   ORFNames=Amme_141_010 {ECO:0000313|EMBL:GAJ30494.1};
OS   Acidomonas methanolica NBRC 104435.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidomonas.
OX   NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ30494.1, ECO:0000313|Proteomes:UP000019760};
RN   [1] {ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX   PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
RN   [2] {ECO:0000313|EMBL:GAJ30494.1, ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|EMBL:GAJ30494.1,
RC   ECO:0000313|Proteomes:UP000019760};
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
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:GAJ30494.1}.
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DR   EMBL; BAND01000140; GAJ30494.1; -; Genomic_DNA.
DR   RefSeq; WP_042061632.1; NZ_BJVB01000051.1.
DR   AlphaFoldDB; A0A023D8Q1; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000019760; 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:UP000019760}.
FT   DOMAIN          14..303
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   309 AA;  31939 MW;  9175BF54D1AA143B CRC64;
     MPHDGAPDIL VPDVLVIESL PPAAQAELER RHATHRFTSL KALHAVAEGI RAVVTGGGTG
     LDPAIMGALP GLRLIAVNGV GTDRIDLVEA ERRGIAVSTT RGLLDADVAD LAMGLMLDVM
     RGISANDRFV RAGEWLKGGP PLGDAITGKK LGIVGLGAIG EGIARRGAAF GMRIAYHTRR
     EKPGSSYTYY SDIVALAHWC DVLVLALPGG PATSGLVNRA VIDAIGPQGY LVNVARGSVV
     DEPELVDALK NGRLGGAGLD VFAHEPQVPE ALLGLENVVL QAHRGSATKE VRAAMAAHVI
     AALDGLAGS
//
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