ID A0A1A7BK27_9SPHN Unreviewed; 312 AA.
AC A0A1A7BK27;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:OBV12081.1};
GN ORFNames=I603_0212 {ECO:0000313|EMBL:OBV12081.1};
OS Erythrobacter dokdonensis DSW-74.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1300349 {ECO:0000313|EMBL:OBV12081.1, ECO:0000313|Proteomes:UP000092484};
RN [1] {ECO:0000313|EMBL:OBV12081.1, ECO:0000313|Proteomes:UP000092484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSW-74 {ECO:0000313|EMBL:OBV12081.1,
RC ECO:0000313|Proteomes:UP000092484};
RA Kim J.F., Song J.Y.;
RT "Genome sequence of Porphyrobacter dokdonensis DSW-74.";
RL Submitted (JUN-2016) 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:OBV12081.1}.
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DR EMBL; LZYB01000001; OBV12081.1; -; Genomic_DNA.
DR RefSeq; WP_068861970.1; NZ_LZYB01000001.1.
DR AlphaFoldDB; A0A1A7BK27; -.
DR STRING; 1300349.I603_0212; -.
DR PATRIC; fig|1300349.4.peg.208; -.
DR Proteomes; UP000092484; 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; IPR029753; D-isomer_DH_CS.
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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 13..302
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..273
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34337 MW; 36587578BE45FC57 CRC64;
MTKLAISGLI RPMLEPRLPQ GLDVRWFMTH EEAMEAVSDA EIGWFDMNDQ KAMAETLIAA
KKLKWLNSIY AGLDFLPMDV LIERGITVTN GAGINAITIA EYVVMGMLNI AKGYREVVRA
QDRHEWLLDS PGKRELAGSK ALLLGYGAIG KLIQPRLEAF DVAVSVVRRS GGEGTLRPDE
WRARLGEFDW VILAVPATPE TEGMIGAEEL AAMKSDCVIV NIARGSVIDQ TALVEALEKK
AIGGAFLDVT TPEPLPADHP LWSLANAHVT MHLSGRAQDK MFVRSADRFL DNLDKYLRGE
PVAPVFDPRL GY
//
