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Database: UniProt
Entry: Q2YYT9
LinkDB: Q2YYT9
Original site: Q2YYT9 
ID   Y2178_STAAB             Reviewed;         317 AA.
AC   Q2YYT9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   28-MAR-2018, entry version 83.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SAB2178;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SAB2178;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AJ938182; CAI81867.1; -; Genomic_DNA.
DR   RefSeq; WP_000417010.1; NC_007622.1.
DR   ProteinModelPortal; Q2YYT9; -.
DR   SMR; Q2YYT9; -.
DR   EnsemblBacteria; CAI81867; CAI81867; SAB2178.
DR   KEGG; sab:SAB2178; -.
DR   HOGENOM; HOG000136700; -.
DR   OMA; KWIAHNG; -.
DR   BioCyc; SAUR273036:G1G1D-2428-MONOMER; -.
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; 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.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    317       Putative 2-hydroxyacid dehydrogenase
FT                                SAB2178.
FT                                /FTId=PRO_0000312182.
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;  34689 MW;  49D41FDFA2A10B07 CRC64;
     MEKVYVAGAI PEVGLKLLQE HFEVEMYEGK GLVDKDTLIK GVKNATALIS LLSTNVDKDV
     IDAGKDLKII ANYGAGFNNI DIEYAREKSI DVTNTPKAST NATADLTIGL VLAIARRIVE
     GDQLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGSAV ARRARAFDMD VLYTGPNRKE
     EKEREIGAKY VDLDTLLKNA DFITINAAYN PKMHHLIDTE QFKMMKSTAY LINASRGPIV
     HEQALVQALK DNEIEGAALD VYEFEPDITD DLKSLNNVVL TPHIGNATFE ARDMMSKIVA
     NAAISAVQGE KPQFVVN
//
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