ID D8MMU4_ERWBE Unreviewed; 315 AA.
AC D8MMU4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:CAX58151.1};
GN OrderedLocusNames=EbC_06200 {ECO:0000313|EMBL:CAX58151.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX58151.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX58151.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FP236843; CAX58151.1; -; Genomic_DNA.
DR RefSeq; WP_013200656.1; NC_014306.1.
DR AlphaFoldDB; D8MMU4; -.
DR STRING; 634500.EbC_06200; -.
DR KEGG; ebi:EbC_06200; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OMA; EQALFMM; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; cd12175; 2-Hacid_dh_11; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 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|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT DOMAIN 25..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 33435 MW; 33B53A18D55FBBC8 CRC64;
MRVLIAAEEN AWGGMIQQFR HTLPDVEFTA SAGHAAESLA GYDALIPGMA KVTPDLLKTA
DRLKLIQQAG AGLEGVDLAS AKALGIQVAN VPSDRSGNAD SVAELGIWMM IGLARKAREI
PEMIATRQLG LPVGMGLMGK TVGLVGLGGI GKALAKRLAP FGVRLIGVKR TADQAFAKAH
QLDWLGNMAH LPALLNDADF VILSLPDNAD TRHIIDETAL AQMKPGSYLI NLGRGGLIEK
QALLAALEVN HLAGAGLDVF WQEPPEPDDA LFQYNVIATP HIGGVTDNSL NGNVAGVCEN
LRRLRDGEEI LNRWA
//