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Database: UniProt
Entry: B5Y201_KLEP3
LinkDB: B5Y201_KLEP3
Original site: B5Y201_KLEP3 
ID   B5Y201_KLEP3            Unreviewed;       316 AA.
AC   B5Y201;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:ACI09863.1};
GN   OrderedLocusNames=KPK_4701 {ECO:0000313|EMBL:ACI09863.1};
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI09863.1, ECO:0000313|Proteomes:UP000001734};
RN   [1] {ECO:0000313|EMBL:ACI09863.1, ECO:0000313|Proteomes:UP000001734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342 {ECO:0000313|EMBL:ACI09863.1,
RC   ECO:0000313|Proteomes:UP000001734};
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP000964; ACI09863.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5Y201; -.
DR   KEGG; kpe:KPK_4701; -.
DR   HOGENOM; CLU_019796_1_2_6; -.
DR   BioCyc; KPNE507522:GI0B-4682-MONOMER; -.
DR   Proteomes; UP000001734; Chromosome.
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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          37..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..284
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   316 AA;  33714 MW;  5350D22655659C3A CRC64;
     MKSVIPRAVL LVAPVIETLQ LQLAEHFPLL RLYEQDDPIA FLREQGENIA VVVTRGDVGV
     ANSVLELLPQ AGLIAIFGVG TDAVDLAYAR SRQIAVTITS GVLTNDVADL AMGLLLAGSR
     QLCQGDRFVR EGRWLSGGMP LATQVSGKRI GLLGMGNIGQ AIARRARGFD MQVLYTDRKK
     IAGLDYQWCA DLHTLAHESD FLVIAASGGE ANRGIIDASV FNVMPAHAWL INIARGSLVD
     EKALIHALQN GVIAGAGLDV FEQEPQVPAA LIALDNVVLQ PHVASATQET RQKMSEVVFA
     NVAAWFAGAA LPNAID
//
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