GenomeNet

Database: UniProt
Entry: Q5HLU4
LinkDB: Q5HLU4
Original site: Q5HLU4 
ID   Y1888_STAEQ             Reviewed;         317 AA.
AC   Q5HLU4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JAN-2019, entry version 91.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SERP1888;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SERP1888;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; CP000029; AAW55277.1; -; Genomic_DNA.
DR   RefSeq; WP_001832639.1; NC_002976.3.
DR   ProteinModelPortal; Q5HLU4; -.
DR   SMR; Q5HLU4; -.
DR   STRING; 176279.SERP1888; -.
DR   EnsemblBacteria; AAW55277; AAW55277; SERP1888.
DR   KEGG; ser:SERP1888; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; SEPI176279:G1G46-1954-MONOMER; -.
DR   Proteomes; UP000000531; 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   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   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    317       Putative 2-hydroxyacid dehydrogenase
FT                                SERP1888.
FT                                /FTId=PRO_0000312189.
FT   NP_BIND     155    156       NAD. {ECO:0000250}.
FT   NP_BIND     234    236       NAD. {ECO:0000250}.
FT   NP_BIND     283    286       NAD. {ECO:0000250}.
FT   ACT_SITE    236    236       {ECO:0000250}.
FT   ACT_SITE    265    265       {ECO:0000250}.
FT   ACT_SITE    283    283       Proton donor. {ECO:0000250}.
FT   BINDING     260    260       NAD. {ECO:0000250}.
SQ   SEQUENCE   317 AA;  34736 MW;  606478610CD419DF CRC64;
     MTKVYIAGAI PEVGLNLLKE HFEVDMYDGE GLIDKETLKK GVEHADALIS LLSTSVDKDI
     IDSANNLKII ANYGAGFNNI DVEYARQQNI DVTNTPHAST NATADLTIGL ILSVARRIVE
     GDHLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGGAV AKRARAFDMD VLYTGPHRKE
     EKERDIGAKY VDLDTLLKNA DFITINAAYN PSLHHMIDTE QFNKMKSTAY LINAGRGPIV
     NEQSLVEALD NKAIEGAALD VYEFEPEITD ALKSFKNVVL TPHIGNATFE ARDMMAKIVA
     NDTIKKLNGD EPQFIVN
//
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