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Database: UniProt
Entry: D8MMU4_ERWBE
LinkDB: D8MMU4_ERWBE
Original site: D8MMU4_ERWBE 
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
//
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